NMNAT2

Nicotinamide nucleotide adenylyltransferase 2
Identifiers
Symbols	NMNAT2; C1orf15; KIAA0479; MGC2756; PNAT2
External IDs	OMIM: 608701 MGI: 2444155 HomoloGene: 75037 GeneCards: NMNAT2 Gene
Gene Ontology Molecular function • nucleotide binding • nicotinamide-nucleotide adenylyltransferase activity • nicotinate-nucleotide adenylyltransferase activity • ATP binding • transferase activity • nucleotidyltransferase activity Cellular component • Golgi membrane • nucleus • cytoplasm • Golgi apparatus Biological process • vitamin metabolic process • water-soluble vitamin metabolic process • biosynthetic process • NAD biosynthetic process • pyridine nucleotide biosynthetic process • NAD metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	23057	226518
Ensembl	ENSG00000157064	ENSMUSG00000042751
UniProt	Q9BZQ4	Q5HZI3
RefSeq (mRNA)	NM_015039.3	NM_175460.3
RefSeq (protein)	NP_055854.1	NP_780669.1
Location (UCSC)	Chr 1: 183.22 – 183.39 Mb	Chr 1: 154.8 – 154.97 Mb
PubMed search	[1]	[2]

Nicotinamide mononucleotide adenylyltransferase 2 is an enzyme that in humans is encoded by the NMNAT2 gene.^[1][2][3]

This gene product belongs to the nicotinamide mononucleotide adenylyltransferase (NMNAT) enzyme family, members of which catalyze an essential step in NAD (NADP) biosynthetic pathway. Unlike the other human family member, which is localized to the nucleus, and is ubiquitously expressed; this enzyme is cytoplasmic, and is predominantly expressed in the brain. Two transcript variants encoding different isoforms have been found for this gene.^[3]

References

1. ^ Sood R, Bonner TI, Makalowska I, Stephan DA, Robbins CM, Connors TD, Morgenbesser SD, Su K, Faruque MU, Pinkett H, Graham C, Baxevanis AD, Klinger KW, Landes GM, Trent JM, Carpten JD (Apr 2001). "Cloning and characterization of 13 novel transcripts and the human RGS8 gene from the 1q25 region encompassing the hereditary prostate cancer (HPC1) locus". Genomics 73 (2): 211–22. doi:10.1006/geno.2001.6500. PMID 11318611. 
2. ^ Raffaelli N, Sorci L, Amici A, Emanuelli M, Mazzola F, Magni G (Oct 2002). "Identification of a novel human nicotinamide mononucleotide adenylyltransferase". Biochem Biophys Res Commun 297 (4): 835–40. doi:10.1016/S0006-291X(02)02285-4. PMID 12359228. 
3. ^ ^{a b} "Entrez Gene: NMNAT2 nicotinamide nucleotide adenylyltransferase 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23057. 

Further reading

• Seki N, Ohira M, Nagase T, et al. (1998). "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain". DNA Res. 4 (5): 345–9. doi:10.1093/dnares/4.5.345. PMID 9455484. 
• 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. 
• 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. PMC 1223862. PMID 14516279. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1223862. 
• 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. 
• 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. 
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414. 
• Sorci L, Cimadamore F, Scotti S, et al. (2007). "Initial-rate kinetics of human NMN-adenylyltransferases: substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis". Biochemistry 46 (16): 4912–22. doi:10.1021/bi6023379. PMID 17402747.