Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P43490

- NAMPT_HUMAN

UniProt

P43490 - NAMPT_HUMAN

Protein

Nicotinamide phosphoribosyltransferase

Gene

NAMPT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.1 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
    4. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Molecular functioni

    Cytokine, Glycosyltransferase, Transferase

    Keywords - Biological processi

    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. Cytoplasm By similarity. Secreted
    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.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular space Source: UniProtKB-KW
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: UniProtKB-SubCell

    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

    ArrayExpressiP43490.
    BgeeiP43490.
    CleanExiHS_NAMPT.
    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. 21 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 – 133
    Beta strandi14 – 163
    Helixi17 – 248
    Beta strandi30 – 3910
    Beta strandi56 – 583
    Helixi62 – 698
    Helixi77 – 9115
    Helixi98 – 10811
    Beta strandi114 – 1185
    Beta strandi124 – 1263
    Beta strandi129 – 13810
    Helixi139 – 1413
    Helixi144 – 1474
    Helixi149 – 1535
    Helixi156 – 18025
    Helixi186 – 1883
    Beta strandi189 – 1924
    Helixi195 – 1973
    Helixi201 – 21111
    Turni212 – 2143
    Beta strandi216 – 2205
    Helixi222 – 2309
    Beta strandi234 – 2363
    Helixi247 – 2515
    Helixi255 – 2573
    Helixi258 – 26811
    Beta strandi270 – 2723
    Beta strandi274 – 2774
    Helixi283 – 2886
    Helixi289 – 2946
    Helixi296 – 2994
    Beta strandi308 – 3114
    Helixi317 – 33115
    Beta strandi338 – 3403
    Beta strandi348 – 3525
    Helixi358 – 37013
    Helixi375 – 3773
    Beta strandi378 – 3836
    Helixi384 – 3874
    Turni392 – 3965
    Beta strandi397 – 40610
    Beta strandi409 – 4124
    Helixi421 – 4233
    Beta strandi431 – 4344
    Beta strandi440 – 4434
    Helixi447 – 4504
    Beta strandi453 – 4553
    Beta strandi459 – 4635
    Helixi473 – 4797
    Turni483 – 4853

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MNPAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKLR    50
    KVKYEETVFY GLQYILNKYL KGKVVTKEKI QEAKDVYKEH FQDDVFNEKG 100
    WNYILEKYDG HLPIEIKAVP EGFVIPRGNV LFTVENTDPE CYWLTNWIET 150
    ILVQSWYPIT VATNSREQKK ILAKYLLETS GNLDGLEYKL HDFGYRGVSS 200
    QETAGIGASA HLVNFKGTDT VAGLALIKKY YGTKDPVPGY SVPAAEHSTI 250
    TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV 300
    SRSTQAPLII RPDSGNPLDT VLKVLEILGK KFPVTENSKG YKLLPPYLRV 350
    IQGDGVDINT LQEIVEGMKQ KMWSIENIAF GSGGGLLQKL TRDLLNCSFK 400
    CSYVVTNGLG INVFKDPVAD PNKRSKKGRL SLHRTPAGNF VTLEEGKGDL 450
    EEYGQDLLHT VFKNGKVTKS YSFDEIRKNA QLNIELEAAH H 491
    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.
    The sequence EAL24400.1 differs from that shown. Reason: Erroneous gene model prediction.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 21 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.
    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

    ArrayExpressi P43490.
    Bgeei P43490.
    CleanExi HS_NAMPT.
    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

    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: October 1, 2014
    This is version 137 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