NEU2

From Wikipedia, the free encyclopedia

Sialidase 2 (cytosolic sialidase)

PDB rendering based on 1snt.

Available structures: 1snt, 1so7, 1vcu, 2f0z, 2f10, 2f11, 2f12, 2f13, 2f24, 2f25, 2f26, 2f27, 2f28, 2f29

Identifiers

Symbol(s)

NEU2; MGC129579; SIAL2

External IDs

OMIM: 605528 MGI: 1344417 HomoloGene: 3927

Gene ontology
Molecular Function:	• exo-alpha-sialidase activity • hydrolase activity, acting on glycosyl bonds
Cellular Component:	• cytoplasm
Biological Process:	• metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_005383 (mRNA)
NP_005374 (protein)

NM_015750 (mRNA)
NP_056565 (protein)

Location

Chr 2: 233.61 - 233.61 Mb

n/a

Pubmed search

[1]

[2]

Sialidase 2 (cytosolic sialidase), also known as NEU2, is a human gene.^[1]

This gene belongs to a family of glycohydrolytic enzymes which remove sialic acid residues from glycoproteins and glycolipids. Expression studies in COS7 cells confirmed that this gene encodes a functional sialidase. Its cytosolic localization was demonstrated by cell fractionation experiments.^[1]

[edit] References

^ ^a ^b Entrez Gene: NEU2 sialidase 2 (cytosolic sialidase).

[edit] Further reading

Li CY, Yu Q, Ye ZQ, et al. (2007). "A nonsynonymous SNP in human cytosolic sialidase in a small Asian population results in reduced enzyme activity: potential link with severe adverse reactions to oseltamivir.". Cell Res. 17 (4): 357-62. doi:10.1038/cr.2007.27. PMID 17426694.
Chavas LM, Tringali C, Fusi P, et al. (2005). "Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition.". J. Biol. Chem. 280 (1): 469-75. doi:10.1074/jbc.M411506200. PMID 15501818.
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.
Tringali C, Papini N, Fusi P, et al. (2004). "Properties of recombinant human cytosolic sialidase HsNEU2. The enzyme hydrolyzes monomerically dispersed GM1 ganglioside molecules.". J. Biol. Chem. 279 (5): 3169-79. doi:10.1074/jbc.M308381200. PMID 14613940.
Hart ML, Saifuddin M, Uemura K, et al. (2003). "High mannose glycans and sialic acid on gp120 regulate binding of mannose-binding lectin (MBL) to HIV type 1.". AIDS Res. Hum. Retroviruses 18 (17): 1311-7. doi:10.1089/088922202320886352. PMID 12487819.
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.
Bassi MT, Sperandeo MP, Incerti B, et al. (2000). "SLC7A8, a gene mapping within the lysinuric protein intolerance critical region, encodes a new member of the glycoprotein-associated amino acid transporter family.". Genomics 62 (2): 297-303. doi:10.1006/geno.1999.5978. PMID 10610726.
Monti E, Preti A, Nesti C, et al. (2000). "Expression of a novel human sialidase encoded by the NEU2 gene.". Glycobiology 9 (12): 1313-21. PMID 10561456.
Monti E, Preti A, Rossi E, et al. (1999). "Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases.". Genomics 57 (1): 137-43. doi:10.1006/geno.1999.5749. PMID 10191093.
Hu H, Shioda T, Moriya C, et al. (1996). "Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surface.". J. Virol. 70 (11): 7462-70. PMID 8892864.
Miyagi T, Konno K, Emori Y, et al. (1994). "Molecular cloning and expression of cDNA encoding rat skeletal muscle cytosolic sialidase.". J. Biol. Chem. 268 (35): 26435-40. PMID 8253770.