ST8SIA2

ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2
Identifiers
Symbols	ST8SIA2 ; HsT19690; SIAT8B; ST8SIA-II; STX
External IDs	OMIM: 602546 MGI: 106020 HomoloGene: 4384 GeneCards: ST8SIA2 Gene
Gene ontology Molecular function • alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity • sialic acid binding Cellular component • Golgi membrane • early endosome • integral component of Golgi membrane • recycling endosome Biological process • ganglioside biosynthetic process • carbohydrate metabolic process • cellular protein modification process • protein glycosylation • dolichol-linked oligosaccharide biosynthetic process • N-glycan processing • nervous system development • axon guidance • oligosaccharide metabolic process • protein N-linked glycosylation via asparagine • post-translational protein modification • cellular protein metabolic process • sialylation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8128	20450
Ensembl	ENSG00000140557	ENSMUSG00000025789
UniProt	Q92186	O35696
RefSeq (mRNA)	NM_006011	NM_009181
RefSeq (protein)	NP_006002	NP_033207
Location (UCSC)	Chr 15: 92.39 – 92.47 Mb	Chr 7: 73.94 – 74.01 Mb
PubMed search

Alpha-2,8-sialyltransferase 8B is an enzyme that in humans is encoded by the ST8SIA2 gene.^[1][2]

The protein encoded by this gene is a type II membrane protein that is thought to catalyze the transfer of sialic acid from CMP-sialic acid to N-linked oligosaccharides and glycoproteins. The encoded protein may be found in the Golgi apparatus and may be involved in the production of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). This protein is a member of glycosyltransferase family 29.^[2]

References

1. Scheidegger EP, Sternberg LR, Roth J, Lowe JB (Nov 1995). "A human STX cDNA confers polysialic acid expression in mammalian cells". J Biol Chem 270 (39): 22685–8. doi:10.1074/jbc.270.39.22685. PMID 7559389.
2. "Entrez Gene: ST8SIA2 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2".

Further reading

• Munro S (1995). "An investigation of the role of transmembrane domains in Golgi protein retention". EMBO J. 14 (19): 4695–704. PMC 394566. PMID 7588599.
• Kitagawa H, Paulson JC (1994). "Differential expression of five sialyltransferase genes in human tissues". J. Biol. Chem. 269 (27): 17872–8. PMID 8027041.
• Kojima N, Tachida Y, Yoshida Y, Tsuji S (1996). "Characterization of mouse ST8Sia II (STX) as a neural cell adhesion molecule-specific polysialic acid synthase. Requirement of core alpha1,6-linked fucose and a polypeptide chain for polysialylation". J. Biol. Chem. 271 (32): 19457–63. doi:10.1074/jbc.271.32.19457. PMID 8702635.
• Angata K, Nakayama J, Fredette B, et al. (1997). "Human STX polysialyltransferase forms the embryonic form of the neural cell adhesion molecule. Tissue-specific expression, neurite outgrowth, and chromosomal localization in comparison with another polysialyltransferase, PST". J. Biol. Chem. 272 (11): 7182–90. doi:10.1074/jbc.272.11.7182. PMID 9054414.
• Close BE, Colley KJ (1999). "In vivo autopolysialylation and localization of the polysialyltransferases PST and STX". J. Biol. Chem. 273 (51): 34586–93. doi:10.1074/jbc.273.51.34586. PMID 9852130.
• Angata K, Suzuki M, McAuliffe J, et al. (2000). "Differential biosynthesis of polysialic acid on neural cell adhesion molecule (NCAM) and oligosaccharide acceptors by three distinct alpha 2,8-sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and ST8Sia III". J. Biol. Chem. 275 (24): 18594–601. doi:10.1074/jbc.M910204199. PMID 10766765.
• Close BE, Wilkinson JM, Bohrer TJ, et al. (2002). "The polysialyltransferase ST8Sia II/STX: posttranslational processing and role of autopolysialylation in the polysialylation of neural cell adhesion molecule". Glycobiology 11 (11): 997–1008. doi:10.1093/glycob/11.11.997. PMID 11744634.
• Angata K, Suzuki M, Fukuda M (2002). "ST8Sia II and ST8Sia IV polysialyltransferases exhibit marked differences in utilizing various acceptors containing oligosialic acid and short polysialic acid. The basis for cooperative polysialylation by two enzymes". J. Biol. Chem. 277 (39): 36808–17. doi:10.1074/jbc.M204632200. PMID 12138100.
• 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.
• Clark HF, Gurney AL, Abaya E, et al. (2003). "The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
• Lazzell DR, Belizaire R, Thakur P, et al. (2005). "SV2B regulates synaptotagmin 1 by direct interaction". J. Biol. Chem. 279 (50): 52124–31. doi:10.1074/jbc.M407502200. PMID 15466855.
• 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.
• Beecken WD, Engl T, Ogbomo H, et al. (2005). "Valproic acid modulates NCAM polysialylation and polysialyltransferase mRNA expression in human tumor cells". Int. Immunopharmacol. 5 (4): 757–69. doi:10.1016/j.intimp.2004.12.009. PMID 15710344.
• Arai M, Yamada K, Toyota T, et al. (2006). "Association between polymorphisms in the promoter region of the sialyltransferase 8B (SIAT8B) gene and schizophrenia". Biol. Psychiatry 59 (7): 652–9. doi:10.1016/j.biopsych.2005.08.016. PMID 16229822.