NADSYN1

NAD synthetase 1
Identifiers
Symbols	NADSYN1; FLJ10631; FLJ36703; FLJ40627
External IDs	OMIM: 608285 MGI: 1926164 HomoloGene: 6098 GeneCards: NADSYN1 Gene
EC number	6.3.5.1
Gene Ontology Molecular function • nucleotide binding • NAD+ synthase (glutamine-hydrolyzing) activity • protein binding • ATP binding • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds • ligase activity Cellular component • cytosol Biological process • vitamin metabolic process • water-soluble vitamin metabolic process • nitrogen compound metabolic process • NAD biosynthetic process • NAD metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	55191	78914
Ensembl	ENSG00000172890	ENSMUSG00000031090
UniProt	Q6IA69	Q8BL34
RefSeq (mRNA)	NM_018161	NM_030221.1
RefSeq (protein)	NP_060631	NP_084497.1
Location (UCSC)	Chr 11: 71.16 – 71.24 Mb	Chr 7: 150.98 – 151.01 Mb
PubMed search	[1]	[2]

Glutamine-dependent NAD(+) synthetase is an enzyme that in humans is encoded by the NADSYN1 gene.^[1][2]

Nicotinamide adenine dinucleotide (NAD) is a coenzyme in metabolic redox reactions, a precursor for several cell signaling molecules, and a substrate for protein posttranslational modifications. NAD synthetase (EC 6.3.5.1) catalyzes the final step in the biosynthesis of NAD from nicotinic acid adenine dinucleotide (NaAD).^[2]

References

1. ^ Hara N, Yamada K, Terashima M, Osago H, Shimoyama M, Tsuchiya M (Mar 2003). "Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency". J Biol Chem 278 (13): 10914–21. doi:10.1074/jbc.M209203200. PMID 12547821. 
2. ^ ^{a b} "Entrez Gene: NADSYN1 NAD synthetase 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55191. 

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Dias Neto E, Correa RG, Verjovski-Almeida S, et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16267. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Lehner B, Sanderson CM (2004). "A Protein Interaction Framework for Human mRNA Degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=442147. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.