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; OMA:ST8SIA4 - orthologs
Gene location (Human) Chr. Chromosome 5 (human) [1] Band 5q21.1 Start 100,806,933 bp [1] End 100,903,282 bp [1]
Gene location (Mouse) Chr. Chromosome 1 (mouse) [2] Band 1|1 D Start 95,587,682 bp [2] End 95,667,571 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bronchial epithelial cell blood monocyte trabecular bone cartilage tissue visceral pleura granulocyte bone marrow lymph node amniotic fluid Top expressed in fossa median eminence Rostral migratory stream medial ganglionic eminence blood motor neuron substantia nigra suprachiasmatic nucleus superior cervical ganglion supraoptic nucleus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function sialyltransferase activity sialic acid binding glycosyltransferase activity 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 sialylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7903 20452 Ensembl ENSG00000113532 ENSMUSG00000040710 UniProt Q92187 Q64692 RefSeq (mRNA) NM_005668 NM_175052 NM_001159745 NM_009183 RefSeq (protein) NP_005659 NP_778222 NP_001153217 NP_033209 Location (UCSC) Chr 5: 100.81 – 100.9 Mb Chr 1: 95.59 – 95.67 Mb PubMed search [3] [4]
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

1. GRCh38: Ensembl release 89: ENSG00000113532 – Ensembl, May 2017
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.
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. Bibcode:1995PNAS...92.7031N. doi: 10.1073/pnas.92.15.7031 . PMC   41465 . PMID   7624364.
6. "Entrez Gene: ST8SIA4 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4".

Further reading

• 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. Bibcode:1995Natur.373..715E. 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. Bibcode:2002PNAS...9916899M. 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.