Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P43490

- NAMPT_HUMAN

UniProt

P43490 - NAMPT_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Nicotinamide phosphoribosyltransferase

Gene

NAMPT

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

Functioni

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).By similarity1 Publication

Catalytic activityi

Nicotinamide D-ribonucleotide + diphosphate = nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate.

Enzyme regulationi

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.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei196 – 1961Diphosphate
Binding sitei219 – 2191Nicotinamide ribonucleotide
Binding sitei247 – 2471Diphosphate
Binding sitei311 – 3111Diphosphate
Binding sitei384 – 3841Nicotinamide ribonucleotide; via amide nitrogen
Binding sitei392 – 3921Nicotinamide ribonucleotide

GO - Molecular functioni

  1. cytokine activity Source: ProtInc
  2. nicotinamide phosphoribosyltransferase activity Source: UniProtKB-EC
  3. nicotinate-nucleotide diphosphorylase (carboxylating) activity Source: InterPro

GO - Biological processi

  1. cell-cell signaling Source: ProtInc
  2. circadian regulation of gene expression Source: UniProtKB
  3. NAD biosynthetic process Source: UniProtKB-UniPathway
  4. NAD metabolic process Source: Reactome
  5. nicotinamide metabolic process Source: Reactome
  6. positive regulation of cell proliferation Source: ProtInc
  7. positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
  8. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  9. signal transduction Source: ProtInc
  10. small molecule metabolic process Source: Reactome
  11. vitamin metabolic process Source: Reactome
  12. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Glycosyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, Pyridine nucleotide biosynthesis

Enzyme and pathway databases

ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_11213. Nicotinamide salvaging.
SABIO-RKP43490.
UniPathwayiUPA00253; UER00890.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide phosphoribosyltransferase (EC:2.4.2.12)
Short name:
NAmPRTase
Short name:
Nampt
Alternative name(s):
Pre-B-cell colony-enhancing factor 1
Short name:
Pre-B cell-enhancing factor
Visfatin
Gene namesi
Name:NAMPT
Synonyms:PBEF, PBEF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:30092. NAMPT.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm By similarity. Secreted 1 Publication
Note: Under non-inflammatory conditions, visfatin predominantly exhibits a granular pattern within the nucleus. Secreted by endothelial cells upon IL-1beta stimulation. Abundantly secreted in milk, reaching 100-fold higher concentrations compared to maternal serum.2 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular space Source: UniProtKB-KW
  3. extracellular vesicular exosome Source: UniProtKB
  4. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi219 – 2191D → N or S: No effect on activity towards nicotinamide. Alters specificity, so that the enzyme acquires activity towards nicotinic acid. 1 Publication
Mutagenesisi247 – 2471H → A: Reduces activity towards nicotinamide. 1 Publication
Mutagenesisi311 – 3111R → D: Reduces activity towards nicotinamide. 1 Publication

Organism-specific databases

PharmGKBiPA162396933.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491Nicotinamide phosphoribosyltransferasePRO_0000205863Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP43490.
PaxDbiP43490.
PRIDEiP43490.

PTM databases

PhosphoSiteiP43490.

Expressioni

Tissue specificityi

Expressed in large amounts in bone marrow, liver tissue, and muscle. Also present in heart, placenta, lung, and kidney tissues.

Gene expression databases

BgeeiP43490.
CleanExiHS_NAMPT.
ExpressionAtlasiP43490. baseline and differential.
GenevestigatoriP43490.

Organism-specific databases

HPAiCAB034349.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FTLP027923EBI-2829310,EBI-713279
IFITM3Q016283EBI-2829310,EBI-7932862
MT-ND1P038863EBI-2829310,EBI-1246156

Protein-protein interaction databases

BioGridi115438. 22 interactions.
DIPiDIP-29218N.
IntActiP43490. 10 interactions.
MINTiMINT-4530953.
STRINGi9606.ENSP00000222553.

Structurei

Secondary structure

1
491
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 133Combined sources
Beta strandi14 – 163Combined sources
Helixi17 – 248Combined sources
Beta strandi30 – 3910Combined sources
Beta strandi56 – 583Combined sources
Helixi62 – 698Combined sources
Helixi77 – 9115Combined sources
Helixi98 – 10811Combined sources
Beta strandi114 – 1185Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi129 – 13810Combined sources
Helixi139 – 1413Combined sources
Helixi144 – 1474Combined sources
Helixi149 – 1535Combined sources
Helixi156 – 18025Combined sources
Helixi186 – 1883Combined sources
Beta strandi189 – 1924Combined sources
Helixi195 – 1973Combined sources
Helixi201 – 21111Combined sources
Turni212 – 2143Combined sources
Beta strandi216 – 2205Combined sources
Helixi222 – 2309Combined sources
Beta strandi234 – 2363Combined sources
Helixi247 – 2515Combined sources
Helixi255 – 2573Combined sources
Helixi258 – 26811Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi274 – 2774Combined sources
Helixi283 – 2886Combined sources
Helixi289 – 2946Combined sources
Helixi296 – 2994Combined sources
Beta strandi308 – 3114Combined sources
Helixi317 – 33115Combined sources
Beta strandi338 – 3403Combined sources
Beta strandi348 – 3525Combined sources
Helixi358 – 37013Combined sources
Helixi375 – 3773Combined sources
Beta strandi378 – 3836Combined sources
Helixi384 – 3874Combined sources
Turni392 – 3965Combined sources
Beta strandi397 – 40610Combined sources
Beta strandi409 – 4124Combined sources
Helixi421 – 4233Combined sources
Beta strandi431 – 4344Combined sources
Beta strandi440 – 4434Combined sources
Helixi447 – 4504Combined sources
Beta strandi453 – 4553Combined sources
Beta strandi459 – 4635Combined sources
Helixi473 – 4797Combined sources
Turni483 – 4853Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5BX-ray2.00A/B1-491[»]
2E5CX-ray2.20A/B1-491[»]
2E5DX-ray2.00A/B1-491[»]
2GVGX-ray2.20A/B/C/D/E/F1-491[»]
2GVJX-ray2.10A/B1-491[»]
3DGRX-ray2.10A/B1-484[»]
3DHDX-ray2.00A/B1-484[»]
3DHFX-ray1.80A/B1-484[»]
3DKJX-ray2.00A/B1-484[»]
3DKLX-ray1.89A/B1-484[»]
4JNMX-ray2.20A/B1-491[»]
4JR5X-ray1.91A/B1-491[»]
4KFNX-ray1.60A/B1-491[»]
4KFOX-ray1.60A/B1-491[»]
4KFPX-ray1.84A/B1-491[»]
4L4LX-ray2.12A/B1-491[»]
4L4MX-ray2.44A/B1-491[»]
4LTSX-ray1.69A/B1-491[»]
4LV9X-ray1.81A/B1-491[»]
4LVAX-ray1.55A/B1-491[»]
4LVBX-ray1.84A/B1-491[»]
4LVDX-ray1.75A/B1-491[»]
4LVFX-ray1.50A/B1-491[»]
4LVGX-ray1.70A/B1-491[»]
4LWWX-ray1.64A/B1-491[»]
4M6PX-ray1.75A/B1-491[»]
4M6QX-ray2.41A/B1-491[»]
4N9BX-ray2.86A/B1-491[»]
4N9CX-ray1.75A/B1-491[»]
4N9DX-ray1.70A/B1-491[»]
4N9EX-ray1.72A/B1-491[»]
4O0ZX-ray2.05A/B1-491[»]
4O10X-ray1.55A/B1-491[»]
4O12X-ray2.50A/B1-491[»]
ProteinModelPortaliP43490.
SMRiP43490. Positions 8-489.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43490.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni311 – 3133Nicotinamide ribonucleotide binding
Regioni353 – 3542Nicotinamide ribonucleotide binding

Sequence similaritiesi

Belongs to the NAPRTase family.Curated

Phylogenomic databases

eggNOGiCOG1488.
GeneTreeiENSGT00390000006647.
HOGENOMiHOG000216546.
HOVERGENiHBG000336.
InParanoidiP43490.
KOiK03462.
OMAiKKFPITE.
OrthoDBiEOG7PGDQH.
PhylomeDBiP43490.
TreeFamiTF333530.

Family and domain databases

InterProiIPR007229. Nic_PRibTrfase-Fam.
IPR016471. Nicotinamide_PRibTrfase.
IPR002638. Quinolinate_PRibosylTrfase_C.
[Graphical view]
PANTHERiPTHR11098. PTHR11098. 1 hit.
PTHR11098:SF2. PTHR11098:SF2. 1 hit.
PfamiPF04095. NAPRTase. 1 hit.
[Graphical view]
PIRSFiPIRSF005943. NMPRT. 1 hit.
SUPFAMiSSF51690. SSF51690. 1 hit.

Sequencei

Sequence statusi: Complete.

P43490-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKLR
60 70 80 90 100
KVKYEETVFY GLQYILNKYL KGKVVTKEKI QEAKDVYKEH FQDDVFNEKG
110 120 130 140 150
WNYILEKYDG HLPIEIKAVP EGFVIPRGNV LFTVENTDPE CYWLTNWIET
160 170 180 190 200
ILVQSWYPIT VATNSREQKK ILAKYLLETS GNLDGLEYKL HDFGYRGVSS
210 220 230 240 250
QETAGIGASA HLVNFKGTDT VAGLALIKKY YGTKDPVPGY SVPAAEHSTI
260 270 280 290 300
TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV
310 320 330 340 350
SRSTQAPLII RPDSGNPLDT VLKVLEILGK KFPVTENSKG YKLLPPYLRV
360 370 380 390 400
IQGDGVDINT LQEIVEGMKQ KMWSIENIAF GSGGGLLQKL TRDLLNCSFK
410 420 430 440 450
CSYVVTNGLG INVFKDPVAD PNKRSKKGRL SLHRTPAGNF VTLEEGKGDL
460 470 480 490
EEYGQDLLHT VFKNGKVTKS YSFDEIRKNA QLNIELEAAH H
Length:491
Mass (Da):55,521
Last modified:November 1, 1995 - v1
Checksum:i6BF07B631B589AC0
GO

Sequence cautioni

The sequence AAQ96862.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAL24400.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti176 – 1761L → S in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036614

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02020 mRNA. Translation: AAA17884.1.
AK292851 mRNA. Translation: BAF85540.1.
AC007032 Genomic DNA. Translation: AAF19249.1.
AC007032 Genomic DNA. Translation: AAQ96862.1. Sequence problems.
CH236947 Genomic DNA. Translation: EAL24399.1.
CH236947 Genomic DNA. Translation: EAL24400.1. Sequence problems.
CH471070 Genomic DNA. Translation: EAW83382.1.
BC072439 mRNA. Translation: AAH72439.1.
BC106046 mRNA. Translation: AAI06047.1.
CCDSiCCDS5737.1.
PIRiA55927.
RefSeqiNP_005737.1. NM_005746.2.
XP_005250157.1. XM_005250100.1.
UniGeneiHs.489615.

Genome annotation databases

EnsembliENST00000222553; ENSP00000222553; ENSG00000105835.
ENST00000354289; ENSP00000346242; ENSG00000105835.
GeneIDi10135.
KEGGihsa:10135.
UCSCiuc003vdq.3. human.

Polymorphism databases

DMDMi1172027.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02020 mRNA. Translation: AAA17884.1 .
AK292851 mRNA. Translation: BAF85540.1 .
AC007032 Genomic DNA. Translation: AAF19249.1 .
AC007032 Genomic DNA. Translation: AAQ96862.1 . Sequence problems.
CH236947 Genomic DNA. Translation: EAL24399.1 .
CH236947 Genomic DNA. Translation: EAL24400.1 . Sequence problems.
CH471070 Genomic DNA. Translation: EAW83382.1 .
BC072439 mRNA. Translation: AAH72439.1 .
BC106046 mRNA. Translation: AAI06047.1 .
CCDSi CCDS5737.1.
PIRi A55927.
RefSeqi NP_005737.1. NM_005746.2.
XP_005250157.1. XM_005250100.1.
UniGenei Hs.489615.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2E5B X-ray 2.00 A/B 1-491 [» ]
2E5C X-ray 2.20 A/B 1-491 [» ]
2E5D X-ray 2.00 A/B 1-491 [» ]
2GVG X-ray 2.20 A/B/C/D/E/F 1-491 [» ]
2GVJ X-ray 2.10 A/B 1-491 [» ]
3DGR X-ray 2.10 A/B 1-484 [» ]
3DHD X-ray 2.00 A/B 1-484 [» ]
3DHF X-ray 1.80 A/B 1-484 [» ]
3DKJ X-ray 2.00 A/B 1-484 [» ]
3DKL X-ray 1.89 A/B 1-484 [» ]
4JNM X-ray 2.20 A/B 1-491 [» ]
4JR5 X-ray 1.91 A/B 1-491 [» ]
4KFN X-ray 1.60 A/B 1-491 [» ]
4KFO X-ray 1.60 A/B 1-491 [» ]
4KFP X-ray 1.84 A/B 1-491 [» ]
4L4L X-ray 2.12 A/B 1-491 [» ]
4L4M X-ray 2.44 A/B 1-491 [» ]
4LTS X-ray 1.69 A/B 1-491 [» ]
4LV9 X-ray 1.81 A/B 1-491 [» ]
4LVA X-ray 1.55 A/B 1-491 [» ]
4LVB X-ray 1.84 A/B 1-491 [» ]
4LVD X-ray 1.75 A/B 1-491 [» ]
4LVF X-ray 1.50 A/B 1-491 [» ]
4LVG X-ray 1.70 A/B 1-491 [» ]
4LWW X-ray 1.64 A/B 1-491 [» ]
4M6P X-ray 1.75 A/B 1-491 [» ]
4M6Q X-ray 2.41 A/B 1-491 [» ]
4N9B X-ray 2.86 A/B 1-491 [» ]
4N9C X-ray 1.75 A/B 1-491 [» ]
4N9D X-ray 1.70 A/B 1-491 [» ]
4N9E X-ray 1.72 A/B 1-491 [» ]
4O0Z X-ray 2.05 A/B 1-491 [» ]
4O10 X-ray 1.55 A/B 1-491 [» ]
4O12 X-ray 2.50 A/B 1-491 [» ]
ProteinModelPortali P43490.
SMRi P43490. Positions 8-489.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115438. 22 interactions.
DIPi DIP-29218N.
IntActi P43490. 10 interactions.
MINTi MINT-4530953.
STRINGi 9606.ENSP00000222553.

Chemistry

BindingDBi P43490.
ChEMBLi CHEMBL1744525.

PTM databases

PhosphoSitei P43490.

Polymorphism databases

DMDMi 1172027.

Proteomic databases

MaxQBi P43490.
PaxDbi P43490.
PRIDEi P43490.

Protocols and materials databases

DNASUi 10135.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000222553 ; ENSP00000222553 ; ENSG00000105835 .
ENST00000354289 ; ENSP00000346242 ; ENSG00000105835 .
GeneIDi 10135.
KEGGi hsa:10135.
UCSCi uc003vdq.3. human.

Organism-specific databases

CTDi 10135.
GeneCardsi GC07M105888.
HGNCi HGNC:30092. NAMPT.
HPAi CAB034349.
MIMi 608764. gene.
neXtProti NX_P43490.
PharmGKBi PA162396933.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1488.
GeneTreei ENSGT00390000006647.
HOGENOMi HOG000216546.
HOVERGENi HBG000336.
InParanoidi P43490.
KOi K03462.
OMAi KKFPITE.
OrthoDBi EOG7PGDQH.
PhylomeDBi P43490.
TreeFami TF333530.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00890 .
Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_11213. Nicotinamide salvaging.
SABIO-RK P43490.

Miscellaneous databases

ChiTaRSi NAMPT. human.
EvolutionaryTracei P43490.
GeneWikii Nicotinamide_phosphoribosyltransferase.
GenomeRNAii 10135.
NextBioi 38341.
PROi P43490.
SOURCEi Search...

Gene expression databases

Bgeei P43490.
CleanExi HS_NAMPT.
ExpressionAtlasi P43490. baseline and differential.
Genevestigatori P43490.

Family and domain databases

InterProi IPR007229. Nic_PRibTrfase-Fam.
IPR016471. Nicotinamide_PRibTrfase.
IPR002638. Quinolinate_PRibosylTrfase_C.
[Graphical view ]
PANTHERi PTHR11098. PTHR11098. 1 hit.
PTHR11098:SF2. PTHR11098:SF2. 1 hit.
Pfami PF04095. NAPRTase. 1 hit.
[Graphical view ]
PIRSFi PIRSF005943. NMPRT. 1 hit.
SUPFAMi SSF51690. SSF51690. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the cDNA encoding a novel human pre-B-cell colony-enhancing factor."
    Samal B., Sun Y., Stearns G., Xie C., Suggs S., McNiece I.
    Mol. Cell. Biol. 14:1431-1437(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Blood.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Trachea.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Lung and Skin.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Visfatin/NAMPT: a multifaceted molecule with diverse roles in physiology and pathophysiology."
    Dahl T.B., Holm S., Aukrust P., Halvorsen B.
    Annu. Rev. Nutr. 32:229-243(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  9. "Visfatin is secreted into the breast milk and is correlated with weight changes of the infant after the birth."
    Bienertova-Vasku J., Bienert P., Zlamal F., Tomandl J., Tomandlova M., Dostalova Z., Vasku A.
    Diabetes Res. Clin. Pract. 96:355-361(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Visfatin as a novel mediator released by inflamed human endothelial cells."
    Romacho T., Villalobos L.A., Cercas E., Carraro R., Sanchez-Ferrer C.F., Peiro C.
    PLoS ONE 8:E78283-E78283(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "Molecular basis for the inhibition of human NMPRTase, a novel target for anticancer agents."
    Khan J.A., Tao X., Tong L.
    Nat. Struct. Mol. Biol. 13:582-588(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE; PRODUCT AND INHIBITOR FK866, ENZYME REGULATION, MUTAGENESIS OF ASP-219; HIS-247 AND ARG-311, SUBUNIT.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-176.

Entry informationi

Entry nameiNAMPT_HUMAN
AccessioniPrimary (citable) accession number: P43490
Secondary accession number(s): A4D0Q9
, A4D0R0, Q3KQV0, Q8WW95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 139 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3