NMNAT1

Nicotinamide nucleotide adenylyltransferase 1
File:PBB Protein NMNAT1 image.jpg PDB rendering based on 1gzu.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1gzu​, 1kku​, 1kqn​, 1kqo​, 1kr2​
Identifiers
Symbols	NMNAT1 ; NMNAT; PNAT-1; PNAT1
External IDs	Template:OMIM5 Template:MGI HomoloGene: 39074
EC number	2.7.7.1
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO Template:GNF GO
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Nicotinamide nucleotide adenylyltransferase 1, also known as NMNAT1, is a human gene. It is a member of the Nicotinamide-nucleotide adenylyltransferases.

The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP-ribosylation, histone deacetylation, and in some Ca(2+) signaling pathways. NMNAT (EC 2.7.7.1) is a central enzyme in NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD (Zhang et al., 2003).[supplied by OMIM]

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. 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. PMID 9373149.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Emanuelli M, Carnevali F, Saccucci F; et al. (2001). "Molecular cloning, chromosomal localization, tissue mRNA levels, bacterial expression, and enzymatic properties of human NMN adenylyltransferase". J. Biol. Chem. 276 (1): 406–12. doi:10.1074/jbc.M008700200. PMID 11027696.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Schweiger M, Hennig K, Lerner F; et al. (2001). "Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis". FEBS Lett. 492 (1–2): 95–100. PMID 11248244.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Garavaglia S, D'Angelo I, Emanuelli M; et al. (2002). "Structure of human NMN adenylyltransferase. A key nuclear enzyme for NAD homeostasis". J. Biol. Chem. 277 (10): 8524–30. doi:10.1074/jbc.M111589200. PMID 11751893.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Werner E, Ziegler M, Lerner F; et al. (2002). "Crystallization and preliminary X-ray analysis of human nicotinamide mononucleotide adenylyltransferase (NMNAT)". Acta Crystallogr. D Biol. Crystallogr. 58 (Pt 1): 140–2. PMID 11752792.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Zhou T, Kurnasov O, Tomchick DR; et al. (2002). "Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin". J. Biol. Chem. 277 (15): 13148–54. doi:10.1074/jbc.M111469200. PMID 11788603.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Fernando FS, Conforti L, Tosi S; et al. (2002). "Human homologue of a gene mutated in the slow Wallerian degeneration (C57BL/Wld(s)) mouse". Gene. 284 (1–2): 23–9. PMID 11891043.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Werner E, Ziegler M, Lerner F; et al. (2002). "Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN". FEBS Lett. 516 (1–3): 239–44. PMID 11959140.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Raffaelli N, Sorci L, Amici A; et al. (2002). "Identification of a novel human nicotinamide mononucleotide adenylyltransferase". Biochem. Biophys. Res. Commun. 297 (4): 835–40. PMID 12359228.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Zhang X, Kurnasov OV, Karthikeyan S; et al. (2003). "Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis". J. Biol. Chem. 278 (15): 13503–11. doi:10.1074/jbc.M300073200. PMID 12574164.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yalowitz JA, Xiao S, Biju MP; et al. (2004). "Characterization of human brain nicotinamide 5'-mononucleotide adenylyltransferase-2 and expression in human pancreas". Biochem. J. 377 (Pt 2): 317–26. doi:10.1042/BJ20030518. PMID 14516279.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Suzuki Y, Yamashita R, Shirota M; et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMID 15342556.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Berger F, Lau C, Dahlmann M, Ziegler M (2006). "Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms". J. Biol. Chem. 280 (43): 36334–41. doi:10.1074/jbc.M508660200. PMID 16118205.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Olsen JV, Blagoev B, Gnad F; et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Berger F, Lau C, Ziegler M (2007). "Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1". Proc. Natl. Acad. Sci. U.S.A. 104 (10): 3765–70. doi:10.1073/pnas.0609211104. PMID 17360427.CS1 maint: Multiple names: authors list (link)