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ST8SIA4

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

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	100,806,933bp^[1]
Band	5q21.1	End	100,903,282bp^[1]

Gene location (Mouse)

Chr.	Chromosome 1 (mouse)^[2]

Band	1\|1 D	Start	95,587,682bp^[2]
Band	1\|1 D	End	95,667,571bp^[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 anenzyme that in humans is encoded by theST8SIA4gene.^[5]^[6]

The protein encoded by this gene catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis ofpolysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). The encoded protein, which is a member ofglycosyltransferase 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

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000113532 –Ensembl, May 2017
^^a ^b ^cGRCm38: 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.Bibcode:1995PNAS...92.7031N.doi:10.1073/pnas.92.15.7031.PMC 41465.PMID 7624364.
^^a ^b"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.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.

Transferases:glycosyltransferases (EC 2.4)

2.4.1:Hexosyl-
transferases

Glucosyl-	Phosphorylase Starch Glycogen Cellobiose Myo- Glycogen synthase Debranching enzyme Branching enzyme 1,3-Beta-glucan synthase Ceramide glucosyltransferase N-glycosyltransferase
Galactosyl-	Lactose synthase B-N-acetylglucosaminyl-glycopeptide b-1,4-galactosyltransferase Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase (C1GALT1)
Glucuronosyl-	B3GAT1 B3GAT2 B3GAT3 UGT1A1 UGT1A3 UGT1A4 UGT1A5 UGT1A6 UGT1A7 UGT1A8 UGT1A9 UGT1A10 UGT2A1 UGT2A2 UGT2A3 UGT2B4 UGT2B7 UGT2B10 UGT2B11 UGT2B15 UGT2B17 UGT2B28 Hyaluronan synthase:HAS1 HAS2 HAS3
Fucosyl-	POFUT1 POFUT2 FUT1 FUT2 FUT3 FUT4 FUT5 FUT6 FUT7 FUT8 FUT9 FUT10 FUT11
Mannosyl-	Dolichyl-phosphate-mannose-protein mannosyltransferase POMT1 POMT2 DPM1 DPM3 ALG1 ALG2 ALG3 ALG6 ALG8 ALG9 ALG12

2.4.2:Pentosyl-
transferases

Ribose

ADP-ribosyltransferase	NAD⁺:diphthamide ADP-ribosyltransferase Diphtheria toxin Pseudomonas exotoxin NAD(P)⁺:arginine ADP-ribosyltransferase Pertussis toxin Cholera toxin Poly ADP ribose polymerase Sirtuin
Phosphoribosyltransferase	Adenine phosphoribosyltransferase Hypoxanthine-guanine phosphoribosyltransferase Uracil phosphoribosyltransferase Amidophosphoribosyltransferase
Other	Purine nucleoside phosphorylase:Thymidine phosphorylase ECGF1

Other

2.4.99:Sialyl
transferases

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme 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	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)

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