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ST8SIA2
Identifiers
Aliases	ST8SIA2, HsT19690, SIAT8B, ST8SIA-II, STX, ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2, SIAT8-B, ST8SiaII
External IDs	OMIM: 602546; MGI: 106020; GeneCards: ST8SIA2
Gene location (Human)
Chr.	Chromosome 15 (human)
End	92,468,728 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	73,663,438 bp
RNA expression pattern
	Top expressed in
	ganglionic eminence; ; ventricular zone; ; testicle; ; left ventricle; ; apex of heart; ; prefrontal cortex; ; retinal pigment epithelium; ; hypothalamus; ; gonad; ; cingulate gyrus;
	Top expressed in
	Rostral migratory stream; ; internal carotid artery; ; external carotid artery; ; ganglionic eminence; ; medial ganglionic eminence; ; vestibular sensory epithelium; ; epithelium of lens; ; neural tube; ; ventricular zone; ; utricle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; glycosyltransferase activity; sialyltransferase activity; sialic acid binding; alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity;
Cellular component	integral component of membrane; recycling endosome; Golgi apparatus; membrane; Golgi membrane; early endosome;
Biological process	N-glycan processing; ganglioside biosynthetic process; nervous system development; protein glycosylation; oligosaccharide metabolic process; sialylation; carbohydrate metabolic process;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	8128
	20450
	ENSG00000140557
	ENSMUSG00000025789
	Q92186
	O35696
	NM_006011; NM_001330416
	NM_009181
	NP_001317345; NP_006002; NP_006002.1
	NP_033207
	Wikidata
View/Edit Human	View/Edit Mouse

Alpha-2,8-sialyltransferase 8B is an enzyme that in humans is encoded by the ST8SIA2 gene.^[5]^[6]

Function

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.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000140557 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025789 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Scheidegger EP, Sternberg LR, Roth J, Lowe JB (September 1995). "A human STX cDNA confers polysialic acid expression in mammalian cells". The Journal of Biological Chemistry. 270 (39): 22685–8. doi:10.1074/jbc.270.39.22685. PMID 7559389.
^ ^a ^b "Entrez Gene: ST8SIA2 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2".

Munro S (October 1995). "An investigation of the role of transmembrane domains in Golgi protein retention". The EMBO Journal. 14 (19): 4695–704. doi:10.1002/j.1460-2075.1995.tb00151.x. PMC 394566. PMID 7588599.
Kitagawa H, Paulson JC (July 1994). "Differential expression of five sialyltransferase genes in human tissues". The Journal of Biological Chemistry. 269 (27): 17872–8. doi:10.1016/S0021-9258(17)32390-6. PMID 8027041.
Kojima N, Tachida Y, Yoshida Y, Tsuji S (August 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". The Journal of Biological Chemistry. 271 (32): 19457–63. doi:10.1074/jbc.271.32.19457. PMID 8702635.
Angata K, Nakayama J, Fredette B, Chong K, Ranscht B, Fukuda M (March 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". The Journal of Biological Chemistry. 272 (11): 7182–90. doi:10.1074/jbc.272.11.7182. PMID 9054414.
Close BE, Colley KJ (December 1998). "In vivo autopolysialylation and localization of the polysialyltransferases PST and STX". The Journal of Biological Chemistry. 273 (51): 34586–93. doi:10.1074/jbc.273.51.34586. PMID 9852130.
Angata K, Suzuki M, McAuliffe J, Ding Y, Hindsgaul O, Fukuda M (June 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". The Journal of Biological Chemistry. 275 (24): 18594–601. doi:10.1074/jbc.M910204199. PMID 10766765.
Close BE, Wilkinson JM, Bohrer TJ, Goodwin CP, Broom LJ, Colley KJ (November 2001). "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 (September 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". The Journal of Biological Chemistry. 277 (39): 36808–17. doi:10.1074/jbc.M204632200. PMID 12138100.
Lazzell DR, Belizaire R, Thakur P, Sherry DM, Janz R (December 2004). "SV2B regulates synaptotagmin 1 by direct interaction". The Journal of Biological Chemistry. 279 (50): 52124–31. doi:10.1074/jbc.M407502200. PMID 15466855.
Beecken WD, Engl T, Ogbomo H, Relja B, Cinatl J, Bereiter-Hahn J, Oppermann E, Jonas D, Blaheta RA (April 2005). "Valproic acid modulates NCAM polysialylation and polysialyltransferase mRNA expression in human tumor cells". International Immunopharmacology. 5 (4): 757–69. doi:10.1016/j.intimp.2004.12.009. PMID 15710344.
Arai M, Yamada K, Toyota T, Obata N, Haga S, Yoshida Y, Nakamura K, Minabe Y, Ujike H, Sora I, Ikeda K, Mori N, Yoshikawa T, Itokawa M (April 2006). "Association between polymorphisms in the promoter region of the sialyltransferase 8B (SIAT8B) gene and schizophrenia". Biological Psychiatry. 59 (7): 652–9. doi:10.1016/j.biopsych.2005.08.016. PMID 16229822. S2CID 349683.
Szabo R, Skropeta D, et al. (2017). "Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities". Med. Res. Rev. 37 (2): 210–270. doi:10.1002/med.21407. PMID 27678392. S2CID 26280291.

This article on a gene on human chromosome 15 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000140557 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000025789 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7559389-5] Scheidegger EP, Sternberg LR, Roth J, Lowe JB (September 1995). "A human STX cDNA confers polysialic acid expression in mammalian cells". The Journal of Biological Chemistry. 270 (39): 22685–8. doi:10.1074/jbc.270.39.22685. PMID 7559389.

[entrez-6] "Entrez Gene: ST8SIA2 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2".

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ST8SIA2

Function

References

Further reading

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