NANS

For other uses, see Nans.

Sialic acid synthase is an enzyme that in humans is encoded by the NANS gene.

NANS
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1WVO
Identifiers
Aliases	NANS, HEL-S-100, SAS, N-acetylneuraminate synthase, SEMDG, SEMDCG
External IDs	OMIM: 605202 MGI: 2149820 HomoloGene: 10343 GeneCards: NANS
EC number	2.5.1.57
Gene location (Human) Chr. Chromosome 9 (human) Band 9q22.33 Start 98,056,732 bp End 98,083,077 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4|4 B1 Start 46,489,248 bp End 46,503,632 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in rectum palpebral conjunctiva parotid gland prostate trachea bronchial epithelial cell minor salivary glands pylorus body of stomach thymus Top expressed in left colon submandibular gland lacrimal gland seminal vesicula basilar part of occipital bone parotid gland crypt of lieberkuhn of small intestine prostate internal carotid artery yolk sac More reference expression data BioGPS More reference expression data
Gene ontology Molecular function N-acetylneuraminate synthase activity transferase activity catalytic activity N-acylneuraminate cytidylyltransferase activity N-acylneuraminate-9-phosphate synthase activity Cellular component cytoplasm cytosol extracellular exosome Biological process carbohydrate biosynthetic process CMP-N-acetylneuraminate biosynthetic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 54187 94181 Ensembl ENSG00000095380 ENSMUSG00000028334 UniProt Q9NR45 Q5TBR0 Q99J77 RefSeq (mRNA) NM_018946 NM_053179 RefSeq (protein) NP_061819 NP_444409 Location (UCSC) Chr 9: 98.06 – 98.08 Mb Chr 4: 46.49 – 46.5 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

This gene encodes an enzyme that functions in the biosynthetic pathways of sialic acids. In vitro, the encoded protein uses N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN), respectively. However, it exhibits much higher activity toward the Neu5Ac phosphate product. In insect cells, expression of this gene results in Neu5Ac and KDN production. This gene is related to the E. coli sialic acid synthase gene neuB, and it can partially restore sialic acid synthase activity in an E. coli neuB-negative mutant.

Further reading

• Lolas F (1978). "Event-related slow brain potentials, cognitive processes, and alexithymia". Psychotherapy and Psychosomatics. 30 (2): 116–29. doi:10.1159/000287290. PMID 693772.
• Nakata D, Close BE, Colley KJ, et al. (2000). "Molecular cloning and expression of the mouse N-acetylneuraminic acid 9-phosphate synthase which does not have deaminoneuraminic acid (KDN) 9-phosphate synthase activity". Biochem. Biophys. Res. Commun. 273 (2): 642–8. doi:10.1006/bbrc.2000.2983. PMID 10873658.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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.
• Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. Bibcode:2004Natur.429..369H. doi:10.1038/nature02465. PMC 2734081. PMID 15164053.
• 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.
• Hao J, Balagurumoorthy P, Sarilla S, Sundaramoorthy M (2006). "Cloning, expression, and characterization of sialic acid synthases". Biochem. Biophys. Res. Commun. 338 (3): 1507–14. doi:10.1016/j.bbrc.2005.10.113. PMID 16274664.
• Hamada T, Ito Y, Abe T, et al. (2006). "Solution structure of the antifreeze-like domain of human sialic acid synthase". Protein Sci. 15 (5): 1010–6. doi:10.1110/ps.051700406. PMC 2242509. PMID 16597820.