NAMPT_HUMAN
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 03-AUG-2022, entry version 200.
DE RecName: Full=Nicotinamide phosphoribosyltransferase;
DE Short=NAmPRTase;
DE Short=Nampt;
DE EC=2.4.2.12 {ECO:0000250|UniProtKB:Q99KQ4};
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=8289818; DOI=10.1128/mcb.14.2.1431-1437.1994;
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-B-cell
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., 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., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA 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., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., 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., Mural R.J.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND IDENTIFICATION BY
RP 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 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., Buerckstuemmer T.,
RA 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 physiology
RT 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 weight
RT 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 MASS
RP 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., Meinnel T.,
RA 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24130902; DOI=10.1371/journal.pone.0078283;
RA Romacho T., Villalobos L.A., Cercas E., Carraro R., Sanchez-Ferrer C.F.,
RA Peiro C.;
RT "Visfatin as a novel mediator released by inflamed human endothelial
RT cells.";
RL PLoS ONE 8:E78283-E78283(2013).
RN [14]
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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE; PRODUCT
RP AND INHIBITOR FK866, ACTIVITY REGULATION, MUTAGENESIS OF ASP-219; HIS-247
RP 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 for
RT anticancer agents.";
RL Nat. Struct. Mol. Biol. 13:582-588(2006).
RN [16]
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., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Catalyzes the condensation of nicotinamide with 5-
CC phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an
CC intermediate in the biosynthesis of NAD. It is the rate limiting
CC component in the mammalian NAD biosynthesis pathway. The secreted form
CC behaves both as a cytokine with immunomodulating properties and an
CC adipokine with anti-diabetic properties, it has no enzymatic activity,
CC partly because of lack of activation by ATP, which has a low level in
CC extracellular space and plasma. Plays a role in the modulation of
CC circadian clock function. NAMPT-dependent oscillatory production of NAD
CC regulates oscillation of clock target gene expression by releasing the
CC core 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:
CC Reaction=beta-nicotinamide D-ribonucleotide + diphosphate = 5-phospho-
CC alpha-D-ribose 1-diphosphate + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16149, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.12;
CC Evidence={ECO:0000250|UniProtKB:Q99KQ4};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16151;
CC Evidence={ECO:0000250|UniProtKB:Q99KQ4};
CC -!- ACTIVITY 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 D-
CC 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 P43490; P02792: FTL; NbExp=3; IntAct=EBI-2829310, EBI-713279;
CC P43490; Q01628: IFITM3; NbExp=3; IntAct=EBI-2829310, EBI-7932862;
CC P43490; P03886: MT-ND1; NbExp=3; IntAct=EBI-2829310, EBI-1246156;
CC P43490; P43490: NAMPT; NbExp=5; IntAct=EBI-2829310, EBI-2829310;
CC P43490; Q70CQ1-2: USP49; NbExp=3; IntAct=EBI-2829310, EBI-12133829;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24130902}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q99KQ4}. Secreted {ECO:0000269|PubMed:21741723}.
CC Note=Under non-inflammatory conditions, visfatin predominantly exhibits
CC a granular pattern within the nucleus. Secreted by endothelial cells
CC upon IL-1beta stimulation. Abundantly secreted in milk, reaching 100-
CC fold higher concentrations compared to maternal serum.
CC {ECO:0000269|PubMed:21741723, ECO:0000269|PubMed:24130902}.
CC -!- TISSUE SPECIFICITY: Expressed in large amounts in bone marrow, liver
CC tissue, and muscle. Also present in heart, placenta, lung, and kidney
CC 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 and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NAMPTID43890ch7q22.html";
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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_005250100.2.
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 PDB; 5KIT; X-ray; 1.60 A; A/B=1-491.
DR PDB; 5LX3; X-ray; 2.10 A; A/B=1-491.
DR PDB; 5LX5; X-ray; 1.88 A; A/B=1-491.
DR PDB; 5NSD; X-ray; 2.05 A; A/B=1-491.
DR PDB; 5U2M; X-ray; 1.89 A; A/B=9-485.
DR PDB; 5U2N; X-ray; 1.73 A; A/B=9-485.
DR PDB; 5UPE; X-ray; 1.93 A; A/B=1-491.
DR PDB; 5UPF; X-ray; 1.69 A; A/B=1-491.
DR PDB; 5WI0; X-ray; 2.05 A; A/B=1-491.
DR PDB; 5WI1; X-ray; 1.99 A; A/B=1-491.
DR PDB; 6ATB; X-ray; 2.53 A; A/B/C/D=1-491.
DR PDB; 6AZJ; X-ray; 2.53 A; A/B=8-485.
DR PDB; 6B75; X-ray; 2.53 A; A/B/C/D=1-491.
DR PDB; 6B76; X-ray; 2.44 A; A/B/C/D=1-491.
DR PDB; 6E68; X-ray; 1.50 A; A/B=8-487.
DR PDB; 6PEB; X-ray; 2.46 A; A/B/C/D=2-491.
DR PDB; 6TA0; X-ray; 1.58 A; A/B=1-491.
DR PDB; 6TA2; X-ray; 1.68 A; A/B=1-491.
DR PDB; 6TAC; X-ray; 1.60 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 PDBsum; 5KIT; -.
DR PDBsum; 5LX3; -.
DR PDBsum; 5LX5; -.
DR PDBsum; 5NSD; -.
DR PDBsum; 5U2M; -.
DR PDBsum; 5U2N; -.
DR PDBsum; 5UPE; -.
DR PDBsum; 5UPF; -.
DR PDBsum; 5WI0; -.
DR PDBsum; 5WI1; -.
DR PDBsum; 6ATB; -.
DR PDBsum; 6AZJ; -.
DR PDBsum; 6B75; -.
DR PDBsum; 6B76; -.
DR PDBsum; 6E68; -.
DR PDBsum; 6PEB; -.
DR PDBsum; 6TA0; -.
DR PDBsum; 6TA2; -.
DR PDBsum; 6TAC; -.
DR AlphaFoldDB; P43490; -.
DR SMR; P43490; -.
DR BioGRID; 115438; 99.
DR DIP; DIP-29218N; -.
DR IntAct; P43490; 29.
DR MINT; P43490; -.
DR STRING; 9606.ENSP00000222553; -.
DR BindingDB; P43490; -.
DR ChEMBL; CHEMBL1744525; -.
DR DrugBank; DB12731; Daporinad.
DR DrugBank; DB05217; GMX1777.
DR DrugCentral; P43490; -.
DR GlyGen; P43490; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P43490; -.
DR MetOSite; P43490; -.
DR PhosphoSitePlus; P43490; -.
DR SwissPalm; P43490; -.
DR BioMuta; NAMPT; -.
DR DMDM; 1172027; -.
DR CPTAC; CPTAC-409; -.
DR CPTAC; CPTAC-410; -.
DR EPD; P43490; -.
DR jPOST; P43490; -.
DR MassIVE; P43490; -.
DR MaxQB; P43490; -.
DR PaxDb; P43490; -.
DR PeptideAtlas; P43490; -.
DR PRIDE; P43490; -.
DR ProteomicsDB; 55638; -.
DR Antibodypedia; 17123; 991 antibodies from 44 providers.
DR DNASU; 10135; -.
DR Ensembl; ENST00000222553.8; ENSP00000222553.3; ENSG00000105835.13.
DR Ensembl; ENST00000424768.2; ENSP00000390591.2; ENSG00000105835.13.
DR Ensembl; ENST00000681255.1; ENSP00000506129.1; ENSG00000105835.13.
DR Ensembl; ENST00000681491.1; ENSP00000506540.1; ENSG00000105835.13.
DR GeneID; 10135; -.
DR KEGG; hsa:10135; -.
DR MANE-Select; ENST00000222553.8; ENSP00000222553.3; NM_005746.3; NP_005737.1.
DR UCSC; uc003vdq.4; human.
DR CTD; 10135; -.
DR DisGeNET; 10135; -.
DR GeneCards; NAMPT; -.
DR HGNC; HGNC:30092; NAMPT.
DR HPA; ENSG00000105835; Low tissue specificity.
DR MIM; 608764; gene.
DR neXtProt; NX_P43490; -.
DR OpenTargets; ENSG00000105835; -.
DR PharmGKB; PA162396933; -.
DR VEuPathDB; HostDB:ENSG00000105835; -.
DR eggNOG; ENOG502QSGN; Eukaryota.
DR GeneTree; ENSGT00940000153456; -.
DR HOGENOM; CLU_012550_2_0_1; -.
DR InParanoid; P43490; -.
DR OMA; TFGFAMK; -.
DR OrthoDB; 446086at2759; -.
DR PhylomeDB; P43490; -.
DR TreeFam; TF333530; -.
DR BRENDA; 2.4.2.12; 2681.
DR PathwayCommons; P43490; -.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR Reactome; R-HSA-197264; Nicotinamide salvaging.
DR SABIO-RK; P43490; -.
DR SignaLink; P43490; -.
DR SIGNOR; P43490; -.
DR UniPathway; UPA00253; UER00890.
DR BioGRID-ORCS; 10135; 202 hits in 1079 CRISPR screens.
DR ChiTaRS; NAMPT; human.
DR EvolutionaryTrace; P43490; -.
DR GeneWiki; Nicotinamide_phosphoribosyltransferase; -.
DR GenomeRNAi; 10135; -.
DR Pharos; P43490; Tchem.
DR PRO; PR:P43490; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P43490; protein.
DR Bgee; ENSG00000105835; Expressed in blood and 196 other tissues.
DR ExpressionAtlas; P43490; baseline and differential.
DR Genevisible; P43490; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005125; F:cytokine activity; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0047280; F:nicotinamide phosphoribosyltransferase activity; IBA:GO_Central.
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:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; TAS:Reactome.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd01569; PBEF_like; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041529; DUF5598.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR016471; Nicotinamide_PRibTrfase.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR PANTHER; PTHR43816; PTHR43816; 1.
DR Pfam; PF18127; NAMPT_N; 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; Cytokine; Cytoplasm;
KW Glycosyltransferase; Nucleus; Phosphoprotein;
KW Pyridine nucleotide biosynthesis; Reference proteome; Secreted;
KW Transferase.
FT CHAIN 1..491
FT /note="Nicotinamide phosphoribosyltransferase"
FT /id="PRO_0000205863"
FT BINDING 196
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT BINDING 219
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT BINDING 247
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT BINDING 311..313
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT BINDING 311
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT BINDING 353..354
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT BINDING 384
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT BINDING 392
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 188
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 176
FT /note="L -> S (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036614"
FT MUTAGEN 219
FT /note="D->N,S: No effect on activity towards nicotinamide.
FT Alters specificity, so that the enzyme acquires activity
FT towards nicotinic acid."
FT /evidence="ECO:0000269|PubMed:16783377"
FT MUTAGEN 247
FT /note="H->A: Reduces activity towards nicotinamide."
FT /evidence="ECO:0000269|PubMed:16783377"
FT MUTAGEN 311
FT /note="R->D: Reduces activity towards nicotinamide."
FT /evidence="ECO:0000269|PubMed:16783377"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 30..39
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 77..91
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 156..180
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:5NSD"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:4LVF"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 247..251
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 258..268
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:6B76"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 317..331
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:2GVJ"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:4LVF"
FT TURN 392..396
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 397..406
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:6AZJ"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 447..450
FT /evidence="ECO:0007829|PDB:4LVF"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:4M6P"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:4LVF"
FT HELIX 473..479
FT /evidence="ECO:0007829|PDB:4LVF"
FT TURN 483..485
FT /evidence="ECO:0007829|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
