ID NADK_HUMAN Reviewed; 446 AA. AC O95544; Q9H931; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 07-JUL-2009, entry version 73. DE RecName: Full=NAD kinase; DE EC=2.7.1.23; DE AltName: Full=Poly(P)/ATP NAD kinase; GN Name=NADK; 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], CATALYTIC ACTIVITY, COFACTOR, RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND VARIANT RP LYS-262. RC TISSUE=Fibroblast; RX MEDLINE=21478959; PubMed=11594753; DOI=10.1006/bbrc.2001.5735; RA Lerner F., Niere M., Ludwig A., Ziegler M.; RT "Structural and functional characterization of human NAD kinase."; RL Biochem. Biophys. Res. Commun. 288:69-74(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-262. RC TISSUE=Lymph; 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-48; SER-50 AND RP SER-64, AND MASS SPECTROMETRY. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). CC -!- CATALYTIC ACTIVITY: ATP + NAD(+) = ADP + NADP(+). CC -!- COFACTOR: Divalent metal cations. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.3 mM for ATP; CC KM=0.54 mM for NAD; CC Vmax=6.7 umol/min/mg enzyme; CC pH dependence: CC Optimum pH is 7.5; CC Temperature dependence: CC Optimum temperature is 55 degrees Celsius; CC -!- INTERACTION: CC P63104:YWHAZ; NbExp=1; IntAct=EBI-743949, EBI-347088; CC -!- TISSUE SPECIFICITY: Widely expressed but not detected in skeletal CC muscle. CC -!- SIMILARITY: Belongs to the NAD kinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY090771; AAM01195.1; -; mRNA. DR EMBL; AK023114; BAB14412.1; -; mRNA. DR EMBL; AL031282; CAA20354.1; -; Genomic_DNA. DR EMBL; BC001709; AAH01709.1; -; mRNA. DR IPI; IPI00794844; -. DR RefSeq; NP_075394.3; -. DR UniGene; Hs.654792; -. DR IntAct; O95544; 7. DR PhosphoSite; O95544; -. DR PRIDE; O95544; -. DR Ensembl; ENSG00000008130; Homo sapiens. DR GeneID; 65220; -. DR KEGG; hsa:65220; -. DR UCSC; uc001aic.1; human. DR GeneCards; GC01M001715; -. DR H-InvDB; HIX0000040; -. DR HGNC; HGNC:29831; NADK. DR MIM; 611616; gene. DR PharmGKB; PA142671298; -. DR HOVERGEN; O95544; -. DR BRENDA; 2.7.1.23; 247. DR Reactome; REACT_11193; Metabolism of vitamins and cofactors. DR NextBio; 67354; -. DR ArrayExpress; O95544; -. DR Bgee; O95544; -. DR CleanEx; HS_NADK; -. DR GermOnline; ENSG00000008130; Homo sapiens. DR GO; GO:0005829; C:cytosol; TAS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003951; F:NAD+ kinase activity; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0046034; P:ATP metabolic process; NAS:UniProtKB. DR GO; GO:0019674; P:NAD metabolic process; EXP:Reactome. DR GO; GO:0016310; P:phosphorylation; NAS:UniProtKB. DR InterPro; IPR017438; ATP-NAD_kinase_PpnK-typ_a/b. DR InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_all-b. DR InterPro; IPR002504; ATP_NADK. DR Gene3D; G3DSA:2.60.200.30; ATP-NAD_kinase_PpnK-typ; 1. DR Gene3D; G3DSA:3.40.50.10330; ATP-NAD_kinase_PpnK-typ_a/b; 1. DR PANTHER; PTHR20275; ATP_NADK; 1. DR Pfam; PF01513; NAD_kinase; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Kinase; Metal-binding; NAD; NADP; KW Nucleotide-binding; Phosphoprotein; Polymorphism; Transferase. FT CHAIN 1 446 NAD kinase. FT /FTId=PRO_0000120713. FT COMPBIAS 326 333 Poly-Ala. FT COMPBIAS 437 445 Poly-Glu. FT MOD_RES 46 46 Phosphoserine. FT MOD_RES 48 48 Phosphoserine. FT MOD_RES 50 50 Phosphoserine. FT MOD_RES 64 64 Phosphoserine. FT VARIANT 262 262 N -> K (in dbSNP:rs4751). FT /FTId=VAR_034119. FT CONFLICT 445 445 E -> EE (in Ref. 2; BAB14412). SQ SEQUENCE 446 AA; 49228 MW; 48CE7AF05EDD7E8B CRC64; MEMEQEKMTM NKELSPDAAA YCCSACHGDE TWSYNHPIRG RAKSRSLSAS PALGSTKEFR RTRSLHGPCP VTTFGPKACV LQNPQTIMHI QDPASQRLTW NKSPKSVLVI KKMRDASLLQ PFKELCTHLM EENMIVYVEK KVLEDPAIAS DESFGAVKKK FCTFREDYDD ISNQIDFIIC LGGDGTLLYA SSLFQGSVPP VMAFHLGSLG FLTPFSFENF QSQVTQVIEG NAAVVLRSRL KVRVVKELRG KKTAVHNGLG ENGSQAAGLD MDVGKQAMQY QVLNEVVIDR GPSSYLSNVD VYLDGHLITT VQGDGVIVST PTGSTAYAAA AGASMIHPNV PAIMITPICP HSLSFRPIVV PAGVELKIML SPEARNTAWV SFDGRKRQEI RHGDSISITT SCYPLPSICV RDPVSDWFES LAQCLHWNVR KKQAHFEEEE EEEEEG //