ID NAMPT_HUMAN Reviewed; 491 AA. AC P43490; A4D0Q9; A4D0R0; Q3KQV0; Q8WW95; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 149. DE RecName: Full=Nicotinamide phosphoribosyltransferase; DE Short=NAmPRTase; DE Short=Nampt; DE EC=2.4.2.12; DE AltName: Full=Pre-B-cell colony-enhancing factor 1; DE Short=Pre-B cell-enhancing factor; DE AltName: Full=Visfatin; GN Name=NAMPT; Synonyms=PBEF, PBEF1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Blood; RX PubMed=8289818; RA Samal B., Sun Y., Stearns G., Xie C., Suggs S., McNiece I.; RT "Cloning and characterization of the cDNA encoding a novel human pre- RT B-cell colony-enhancing factor."; RL Mol. Cell. Biol. 14:1431-1437(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., RA Mural R.J., Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP REVIEW. RX PubMed=22462624; DOI=10.1146/annurev-nutr-071811-150746; RA Dahl T.B., Holm S., Aukrust P., Halvorsen B.; RT "Visfatin/NAMPT: a multifaceted molecule with diverse roles in RT physiology and pathophysiology."; RL Annu. Rev. Nutr. 32:229-243(2012). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=21741723; DOI=10.1016/j.diabres.2011.06.009; RA Bienertova-Vasku J., Bienert P., Zlamal F., Tomandl J., Tomandlova M., RA Dostalova Z., Vasku A.; RT "Visfatin is secreted into the breast milk and is correlated with RT weight changes of the infant after the birth."; RL Diabetes Res. Clin. Pract. 96:355-361(2012). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [12] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=24130902; DOI=10.1371/journal.pone.0078283; RA Romacho T., Villalobos L.A., Cercas E., Carraro R., RA Sanchez-Ferrer C.F., Peiro C.; RT "Visfatin as a novel mediator released by inflamed human endothelial RT cells."; RL PLoS ONE 8:E78283-E78283(2013). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE; RP PRODUCT AND INHIBITOR FK866, ENZYME REGULATION, MUTAGENESIS OF RP ASP-219; HIS-247 AND ARG-311, AND SUBUNIT. RX PubMed=16783377; DOI=10.1038/nsmb1105; RA Khan J.A., Tao X., Tong L.; RT "Molecular basis for the inhibition of human NMPRTase, a novel target RT for anticancer agents."; RL Nat. Struct. Mol. Biol. 13:582-588(2006). RN [15] RP VARIANT [LARGE SCALE ANALYSIS] SER-176. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Catalyzes the condensation of nicotinamide with 5- CC phosphoribosyl-1-pyrophosphate to yield nicotinamide CC mononucleotide, an intermediate in the biosynthesis of NAD. It is CC the rate limiting component in the mammalian NAD biosynthesis CC pathway. The secreted form behaves both as a cytokine with CC immunomodulating properties and an adipokine with anti-diabetic CC properties, it has no enzymatic activity, partly because of lack CC of activation by ATP, which has a low level in extracellular space CC and plasma. Plays a role in the modulation of circadian clock CC function. NAMPT-dependent oscillatory production of NAD regulates CC oscillation of clock target gene expression by releasing the core CC clock component: CLOCK-ARNTL/BMAL1 heterodimer from NAD-dependent CC SIRT1-mediated suppression (By similarity). CC {ECO:0000250|UniProtKB:Q99KQ4, ECO:0000269|PubMed:24130902}. CC -!- CATALYTIC ACTIVITY: Nicotinamide D-ribonucleotide + diphosphate = CC nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate. CC -!- ENZYME REGULATION: Inhibited by FK866. FK866 competes for the same CC binding site as nicotinamide, but due to its very low dissociation CC rate, it is essentially an irreversible inhibitor. CC {ECO:0000269|PubMed:16783377}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinamide CC D-ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and CC nicotinamide: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16783377}. CC -!- INTERACTION: CC P02792:FTL; NbExp=3; IntAct=EBI-2829310, EBI-713279; CC Q01628:IFITM3; NbExp=3; IntAct=EBI-2829310, EBI-7932862; CC P03886:MT-ND1; NbExp=3; IntAct=EBI-2829310, EBI-1246156; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24130902}. CC Cytoplasm {ECO:0000250|UniProtKB:Q99KQ4}. Secreted CC {ECO:0000269|PubMed:21741723}. Note=Under non-inflammatory CC conditions, visfatin predominantly exhibits a granular pattern CC within the nucleus. Secreted by endothelial cells upon IL-1beta CC stimulation. Abundantly secreted in milk, reaching 100-fold higher CC concentrations compared to maternal serum. CC {ECO:0000269|PubMed:21741723, ECO:0000269|PubMed:24130902}. CC -!- TISSUE SPECIFICITY: Expressed in large amounts in bone marrow, CC liver tissue, and muscle. Also present in heart, placenta, lung, CC and kidney tissues. CC -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAQ96862.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=EAL24400.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/NAMPTID43890ch7q22.html"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U02020; AAA17884.1; -; mRNA. DR EMBL; AK292851; BAF85540.1; -; mRNA. DR EMBL; AC007032; AAF19249.1; -; Genomic_DNA. DR EMBL; AC007032; AAQ96862.1; ALT_SEQ; Genomic_DNA. DR EMBL; CH236947; EAL24399.1; -; Genomic_DNA. DR EMBL; CH236947; EAL24400.1; ALT_SEQ; Genomic_DNA. DR EMBL; CH471070; EAW83382.1; -; Genomic_DNA. DR EMBL; BC072439; AAH72439.1; -; mRNA. DR EMBL; BC106046; AAI06047.1; -; mRNA. DR CCDS; CCDS5737.1; -. DR PIR; A55927; A55927. DR RefSeq; NP_005737.1; NM_005746.2. DR RefSeq; XP_005250157.1; XM_005250100.1. DR UniGene; Hs.489615; -. DR PDB; 2E5B; X-ray; 2.00 A; A/B=1-491. DR PDB; 2E5C; X-ray; 2.20 A; A/B=1-491. DR PDB; 2E5D; X-ray; 2.00 A; A/B=1-491. DR PDB; 2GVG; X-ray; 2.20 A; A/B/C/D/E/F=1-491. DR PDB; 2GVJ; X-ray; 2.10 A; A/B=1-491. DR PDB; 3DGR; X-ray; 2.10 A; A/B=1-484. DR PDB; 3DHD; X-ray; 2.00 A; A/B=1-484. DR PDB; 3DHF; X-ray; 1.80 A; A/B=1-484. DR PDB; 3DKJ; X-ray; 2.00 A; A/B=1-484. DR PDB; 3DKL; X-ray; 1.89 A; A/B=1-484. DR PDB; 4JNM; X-ray; 2.20 A; A/B=1-491. DR PDB; 4JR5; X-ray; 1.91 A; A/B=1-491. DR PDB; 4KFN; X-ray; 1.60 A; A/B=1-491. DR PDB; 4KFO; X-ray; 1.60 A; A/B=1-491. DR PDB; 4KFP; X-ray; 1.84 A; A/B=1-491. DR PDB; 4L4L; X-ray; 2.12 A; A/B=1-491. DR PDB; 4L4M; X-ray; 2.44 A; A/B=1-491. DR PDB; 4LTS; X-ray; 1.69 A; A/B=1-491. DR PDB; 4LV9; X-ray; 1.81 A; A/B=1-491. DR PDB; 4LVA; X-ray; 1.55 A; A/B=1-491. DR PDB; 4LVB; X-ray; 1.84 A; A/B=1-491. DR PDB; 4LVD; X-ray; 1.75 A; A/B=1-491. DR PDB; 4LVF; X-ray; 1.50 A; A/B=1-491. DR PDB; 4LVG; X-ray; 1.70 A; A/B=1-491. DR PDB; 4LWW; X-ray; 1.64 A; A/B=1-491. DR PDB; 4M6P; X-ray; 1.75 A; A/B=1-491. DR PDB; 4M6Q; X-ray; 2.41 A; A/B=1-491. DR PDB; 4N9B; X-ray; 2.86 A; A/B=1-491. DR PDB; 4N9C; X-ray; 1.75 A; A/B=1-491. DR PDB; 4N9D; X-ray; 1.70 A; A/B=1-491. DR PDB; 4N9E; X-ray; 1.72 A; A/B=1-491. DR PDB; 4O0Z; X-ray; 2.05 A; A/B=1-491. DR PDB; 4O10; X-ray; 1.55 A; A/B=1-491. DR PDB; 4O12; X-ray; 2.50 A; A/B=1-491. DR PDB; 4O13; X-ray; 1.75 A; A/B=1-491. DR PDB; 4O14; X-ray; 1.87 A; A/B=1-491. DR PDB; 4O15; X-ray; 1.80 A; A/B=1-491. DR PDB; 4O16; X-ray; 1.78 A; A=1-491. DR PDB; 4O17; X-ray; 1.82 A; A/B=1-491. DR PDB; 4O18; X-ray; 1.92 A; A/B=1-491. DR PDB; 4O19; X-ray; 1.75 A; A/B=1-491. DR PDB; 4O1A; X-ray; 1.87 A; A/B=1-491. DR PDB; 4O1B; X-ray; 1.65 A; A/B=1-491. DR PDB; 4O1C; X-ray; 2.09 A; A/B=1-491. DR PDB; 4O1D; X-ray; 1.70 A; A/B=1-491. DR PDB; 4O28; X-ray; 2.00 A; A/B=1-491. DR PDB; 4WQ6; X-ray; 1.72 A; A/B=1-491. DR PDBsum; 2E5B; -. DR PDBsum; 2E5C; -. DR PDBsum; 2E5D; -. DR PDBsum; 2GVG; -. DR PDBsum; 2GVJ; -. DR PDBsum; 3DGR; -. DR PDBsum; 3DHD; -. DR PDBsum; 3DHF; -. DR PDBsum; 3DKJ; -. DR PDBsum; 3DKL; -. DR PDBsum; 4JNM; -. DR PDBsum; 4JR5; -. DR PDBsum; 4KFN; -. DR PDBsum; 4KFO; -. DR PDBsum; 4KFP; -. DR PDBsum; 4L4L; -. DR PDBsum; 4L4M; -. DR PDBsum; 4LTS; -. DR PDBsum; 4LV9; -. DR PDBsum; 4LVA; -. DR PDBsum; 4LVB; -. DR PDBsum; 4LVD; -. DR PDBsum; 4LVF; -. DR PDBsum; 4LVG; -. DR PDBsum; 4LWW; -. DR PDBsum; 4M6P; -. DR PDBsum; 4M6Q; -. DR PDBsum; 4N9B; -. DR PDBsum; 4N9C; -. DR PDBsum; 4N9D; -. DR PDBsum; 4N9E; -. DR PDBsum; 4O0Z; -. DR PDBsum; 4O10; -. DR PDBsum; 4O12; -. DR PDBsum; 4O13; -. DR PDBsum; 4O14; -. DR PDBsum; 4O15; -. DR PDBsum; 4O16; -. DR PDBsum; 4O17; -. DR PDBsum; 4O18; -. DR PDBsum; 4O19; -. DR PDBsum; 4O1A; -. DR PDBsum; 4O1B; -. DR PDBsum; 4O1C; -. DR PDBsum; 4O1D; -. DR PDBsum; 4O28; -. DR PDBsum; 4WQ6; -. DR ProteinModelPortal; P43490; -. DR SMR; P43490; 8-489. DR BioGrid; 115438; 25. DR DIP; DIP-29218N; -. DR IntAct; P43490; 10. DR MINT; MINT-4530953; -. DR STRING; 9606.ENSP00000222553; -. DR BindingDB; P43490; -. DR ChEMBL; CHEMBL1744525; -. DR PhosphoSite; P43490; -. DR BioMuta; NAMPT; -. DR DMDM; 1172027; -. DR MaxQB; P43490; -. DR PaxDb; P43490; -. DR PRIDE; P43490; -. DR DNASU; 10135; -. DR Ensembl; ENST00000222553; ENSP00000222553; ENSG00000105835. DR GeneID; 10135; -. DR KEGG; hsa:10135; -. DR UCSC; uc003vdq.3; human. DR CTD; 10135; -. DR GeneCards; NAMPT; -. DR HGNC; HGNC:30092; NAMPT. DR HPA; CAB034349; -. DR HPA; HPA047776; -. DR HPA; HPA057722; -. DR MIM; 608764; gene. DR neXtProt; NX_P43490; -. DR PharmGKB; PA162396933; -. DR eggNOG; ENOG410IEB2; Eukaryota. DR eggNOG; COG1488; LUCA. DR GeneTree; ENSGT00390000006647; -. DR HOGENOM; HOG000216546; -. DR HOVERGEN; HBG000336; -. DR InParanoid; P43490; -. DR KO; K03462; -. DR OMA; KKFPITE; -. DR OrthoDB; EOG7PGDQH; -. DR PhylomeDB; P43490; -. DR TreeFam; TF333530; -. DR BRENDA; 2.4.2.12; 2681. DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression. DR Reactome; R-HSA-197264; Nicotinamide salvaging. DR SABIO-RK; P43490; -. DR UniPathway; UPA00253; UER00890. DR ChiTaRS; NAMPT; human. DR EvolutionaryTrace; P43490; -. DR GeneWiki; Nicotinamide_phosphoribosyltransferase; -. DR GenomeRNAi; 10135; -. DR NextBio; 38341; -. DR PRO; PR:P43490; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; P43490; -. DR CleanEx; HS_NAMPT; -. DR ExpressionAtlas; P43490; baseline and differential. DR Genevisible; P43490; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005125; F:cytokine activity; TAS:ProtInc. DR GO; GO:0008144; F:drug binding; IEA:Ensembl. DR GO; GO:0047280; F:nicotinamide phosphoribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB. DR GO; GO:0007623; P:circadian rhythm; TAS:Reactome. DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019674; P:NAD metabolic process; TAS:Reactome. DR GO; GO:0006769; P:nicotinamide metabolic process; TAS:Reactome. DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc. DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL. DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006766; P:vitamin metabolic process; TAS:Reactome. DR GO; GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome. DR InterPro; IPR007229; Nic_PRibTrfase-Fam. DR InterPro; IPR016471; Nicotinamide_PRibTrfase. DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C. DR PANTHER; PTHR11098; PTHR11098; 1. DR PANTHER; PTHR11098:SF15; PTHR11098:SF15; 1. DR Pfam; PF04095; NAPRTase; 1. DR PIRSF; PIRSF005943; NMPRT; 1. DR SUPFAM; SSF51690; SSF51690; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Biological rhythms; Complete proteome; KW Cytokine; Cytoplasm; Glycosyltransferase; Nucleus; Phosphoprotein; KW Polymorphism; Pyridine nucleotide biosynthesis; Reference proteome; KW Secreted; Transferase. FT CHAIN 1 491 Nicotinamide phosphoribosyltransferase. FT /FTId=PRO_0000205863. FT REGION 311 313 Nicotinamide ribonucleotide binding. FT REGION 353 354 Nicotinamide ribonucleotide binding. FT BINDING 196 196 Diphosphate. FT BINDING 219 219 Nicotinamide ribonucleotide. FT BINDING 247 247 Diphosphate. FT BINDING 311 311 Diphosphate. FT BINDING 384 384 Nicotinamide ribonucleotide; via amide FT nitrogen. FT BINDING 392 392 Nicotinamide ribonucleotide. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000244|PubMed:22223895}. FT MOD_RES 188 188 Phosphotyrosine. FT {ECO:0000244|PubMed:15592455}. FT VARIANT 176 176 L -> S (in a colorectal cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036614. FT MUTAGEN 219 219 D->N,S: No effect on activity towards FT nicotinamide. Alters specificity, so that FT the enzyme acquires activity towards FT nicotinic acid. FT {ECO:0000269|PubMed:16783377}. FT MUTAGEN 247 247 H->A: Reduces activity towards FT nicotinamide. FT {ECO:0000269|PubMed:16783377}. FT MUTAGEN 311 311 R->D: Reduces activity towards FT nicotinamide. FT {ECO:0000269|PubMed:16783377}. FT HELIX 11 13 {ECO:0000244|PDB:4LVF}. FT STRAND 14 16 {ECO:0000244|PDB:4LVF}. FT HELIX 17 24 {ECO:0000244|PDB:4LVF}. FT STRAND 30 39 {ECO:0000244|PDB:4LVF}. FT STRAND 56 58 {ECO:0000244|PDB:4LVF}. FT HELIX 62 69 {ECO:0000244|PDB:4LVF}. FT HELIX 77 91 {ECO:0000244|PDB:4LVF}. FT HELIX 98 108 {ECO:0000244|PDB:4LVF}. FT STRAND 114 118 {ECO:0000244|PDB:4LVF}. FT STRAND 124 126 {ECO:0000244|PDB:4LVF}. FT STRAND 129 138 {ECO:0000244|PDB:4LVF}. FT HELIX 139 141 {ECO:0000244|PDB:4LVF}. FT HELIX 144 147 {ECO:0000244|PDB:4LVF}. FT HELIX 149 153 {ECO:0000244|PDB:4LVF}. FT HELIX 156 180 {ECO:0000244|PDB:4LVF}. FT HELIX 186 188 {ECO:0000244|PDB:4LVF}. FT STRAND 189 192 {ECO:0000244|PDB:4LVF}. FT HELIX 195 197 {ECO:0000244|PDB:4LVF}. FT HELIX 201 211 {ECO:0000244|PDB:4LVF}. FT TURN 212 214 {ECO:0000244|PDB:4LVF}. FT STRAND 216 220 {ECO:0000244|PDB:4LVF}. FT HELIX 222 230 {ECO:0000244|PDB:4LVF}. FT STRAND 234 236 {ECO:0000244|PDB:4LVF}. FT HELIX 247 251 {ECO:0000244|PDB:4LVF}. FT HELIX 255 257 {ECO:0000244|PDB:4LVF}. FT HELIX 258 268 {ECO:0000244|PDB:4LVF}. FT STRAND 270 272 {ECO:0000244|PDB:4LVF}. FT STRAND 274 277 {ECO:0000244|PDB:4LVF}. FT HELIX 283 288 {ECO:0000244|PDB:4LVF}. FT HELIX 289 294 {ECO:0000244|PDB:4LVF}. FT HELIX 296 299 {ECO:0000244|PDB:4LVF}. FT STRAND 308 311 {ECO:0000244|PDB:4LVF}. FT HELIX 317 331 {ECO:0000244|PDB:4LVF}. FT STRAND 338 340 {ECO:0000244|PDB:2GVJ}. FT STRAND 348 352 {ECO:0000244|PDB:4LVF}. FT HELIX 358 370 {ECO:0000244|PDB:4LVF}. FT HELIX 375 377 {ECO:0000244|PDB:4LVF}. FT STRAND 378 383 {ECO:0000244|PDB:4LVF}. FT HELIX 384 387 {ECO:0000244|PDB:4LVF}. FT TURN 392 396 {ECO:0000244|PDB:4LVF}. FT STRAND 397 406 {ECO:0000244|PDB:4LVF}. FT STRAND 409 412 {ECO:0000244|PDB:4LVF}. FT HELIX 421 423 {ECO:0000244|PDB:4LVF}. FT STRAND 431 434 {ECO:0000244|PDB:4LVF}. FT STRAND 440 443 {ECO:0000244|PDB:4LVF}. FT HELIX 447 450 {ECO:0000244|PDB:4LVF}. FT STRAND 453 455 {ECO:0000244|PDB:4M6P}. FT STRAND 459 463 {ECO:0000244|PDB:4LVF}. FT HELIX 473 479 {ECO:0000244|PDB:4LVF}. FT TURN 483 485 {ECO:0000244|PDB:4LVF}. SQ SEQUENCE 491 AA; 55521 MW; 6BF07B631B589AC0 CRC64; MNPAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKLR KVKYEETVFY GLQYILNKYL KGKVVTKEKI QEAKDVYKEH FQDDVFNEKG WNYILEKYDG HLPIEIKAVP EGFVIPRGNV LFTVENTDPE CYWLTNWIET ILVQSWYPIT VATNSREQKK ILAKYLLETS GNLDGLEYKL HDFGYRGVSS QETAGIGASA HLVNFKGTDT VAGLALIKKY YGTKDPVPGY SVPAAEHSTI TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV SRSTQAPLII RPDSGNPLDT VLKVLEILGK KFPVTENSKG YKLLPPYLRV IQGDGVDINT LQEIVEGMKQ KMWSIENIAF GSGGGLLQKL TRDLLNCSFK CSYVVTNGLG INVFKDPVAD PNKRSKKGRL SLHRTPAGNF VTLEEGKGDL EEYGQDLLHT VFKNGKVTKS YSFDEIRKNA QLNIELEAAH H //