ST8SIA4

ST8SIA4
Identifiers
Aliases	ST8SIA4, PST, PST1, SIAT8D, ST8SIA-IV, ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4
External IDs	OMIM: 602547 MGI: 106018 HomoloGene: 4147 GeneCards: ST8SIA4
Gene location (Human)
Chr.	Chromosome 5 (human)[1]
End	100,903,282 bp[1]
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)[2]
End	95,667,571 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• sialyltransferase activity; • sialic acid binding; • transferase activity, transferring glycosyl groups; • transferase activity; • alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity;
Cellular component	• integral component of membrane; • Golgi membrane; • membrane; • Golgi apparatus;
Biological process	• nervous system development; • protein glycosylation; • N-glycan processing; • ganglioside biosynthetic process; • oligosaccharide metabolic process; • cellular protein modification process; • sialylation;
	Sources:Amigo / QuickGO
Orthologs
	7903
	20452
	ENSG00000113532
	ENSMUSG00000040710
	Q92187
	Q64692
	NM_005668; NM_175052
	NM_001159745; NM_009183
	NP_005659; NP_778222
	NP_001153217; NP_033209
	Wikidata
View/Edit Human	View/Edit Mouse

CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase is an enzyme that in humans is encoded by the ST8SIA4 gene.[5][6]

The protein encoded by this gene catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). The encoded protein, which is a member of glycosyltransferase family 29, is a type II membrane protein that may be present in the Golgi apparatus. Two transcript variants encoding different isoforms have been found for this gene.[6]

References

GRCh38: Ensembl release 89: ENSG00000113532 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000040710 - 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.
Nakayama J, Fukuda MN, Fredette B, Ranscht B, Fukuda M (Aug 1995). "Expression cloning of a human polysialyltransferase that forms the polysialylated neural cell adhesion molecule present in embryonic brain". Proc Natl Acad Sci U S A. 92 (15): 7031–5. doi:10.1073/pnas.92.15.7031. PMC 41465. PMID 7624364.
"Entrez Gene: ST8SIA4 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4".

Cohn JA, Noone PG, Jowell PS (2002). "Idiopathic pancreatitis related to CFTR: complex inheritance and identification of a modifier gene". J. Investig. Med. 50 (5): 247S–255S. doi:10.1136/jim-50-suppl5-01. PMID 12227654. S2CID 34017638.
Eckhardt M, Mühlenhoff M, Bethe A, et al. (1995). "Molecular characterization of eukaryotic polysialyltransferase-1". Nature. 373 (6516): 715–8. doi:10.1038/373715a0. PMID 7854457. S2CID 4345323.
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.
Angata K, Suzuki M, Fukuda M (1998). "Differential and cooperative polysialylation of the neural cell adhesion molecule by two polysialyltransferases, PST and STX". J. Biol. Chem. 273 (43): 28524–32. doi:10.1074/jbc.273.43.28524. PMID 9774483.
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.
Close BE, Tao K, Colley KJ (2000). "Polysialyltransferase-1 autopolysialylation is not requisite for polysialylation of neural cell adhesion molecule". J. Biol. Chem. 275 (6): 4484–91. doi:10.1074/jbc.275.6.4484. PMID 10660622.
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.
Angata K, Yen TY, El-Battari A, et al. (2001). "Unique disulfide bond structures found in ST8Sia IV polysialyltransferase are required for its activity". J. Biol. Chem. 276 (18): 15369–77. doi:10.1074/jbc.M100576200. PMID 11279095.
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.
Nałogowska-Głośnicka K, Łacka B, Zychma M, et al. (2002). "[Relationship between SA gene Pst1 polymorphism and predisposition to H-gestosis]". Pol. Arch. Med. Wewn. 107 (1): 7–11. PMID 12046348.
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.
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.
Mendiratta SS, Sekulic N, Lavie A, Colley KJ (2005). "Specific amino acids in the first fibronectin type III repeat of the neural cell adhesion molecule play a role in its recognition and polysialylation by the polysialyltransferase ST8Sia IV/PST". J. Biol. Chem. 280 (37): 32340–8. doi:10.1074/jbc.M506217200. PMID 16027151.
Wang B, Hu H, Yu B (2007). "Molecular characterization of pig ST8Sia IV--a critical gene for the formation of neural cell adhesion molecule and its response to sialic acid supplement in piglets". Nutritional Neuroscience. 9 (3–4): 147–54. doi:10.1080/10284150600903594. PMID 17176637. S2CID 7793568.
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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000113532 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000040710 - 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.

[pmid7624364-5] Nakayama J, Fukuda MN, Fredette B, Ranscht B, Fukuda M (Aug 1995). "Expression cloning of a human polysialyltransferase that forms the polysialylated neural cell adhesion molecule present in embryonic brain". Proc Natl Acad Sci U S A. 92 (15): 7031–5. doi:10.1073/pnas.92.15.7031. PMC 41465. PMID 7624364.

[entrez-6] "Entrez Gene: ST8SIA4 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4".

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

ST8SIA4

References

Further reading