GGDB:

ST8SIA2, ST8 α-N-acetylneuraminide α-2,8-sialyltransferase 2, transfers sialic acid from CMP-sialic acid to the NeuAcα2→3-R and NeuAcα2→6-R structure on glycoproteins, mainly on the neural cell adhesion molecule (NCAM), synthesizing homopolymer of α2,8-linked sialic acid called polysialic acid. ST8SIA2 is also known as STX or SIAT8B or ST8Sia-II. ST8SIA2 also synthesizes polysialic acid on the synaptic cell adhesion molecule (SynCAM 1). ST8SIA2-deficient mice exhibit morphological change of mossy fiber and loss of anxiety. Double deficient mice of ST8SIA2 and ST8SIA4 lose polysiaic acid and die in early neonatal period.

Keyword:

	CMP-Neu5Ac
JCGG-STR014102 GlyTouCan: G00065MO GlyCosmos Glycans: G00065MO		JCGG-STR033514

	CMP-Neu5Ac
JCGG-STR013995 GlyTouCan: G73578JC GlyCosmos Glycans: G73578JC		JCGG-STR033515

Sialyltransferase

GGDB Symbol

ST8SIA2 Alias

Designation

ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2

Organism

Homo sapiens

GeneID

8128

HGNC

ST8SIA2 (10870)

mRNA

NM_006011

map

15q26

Protein

NP_006002

EC#

CAZy

GT29

GlyCosmos Glycogenes

ST8SIA2

OMIM

602546

Disease name

GDGDB

Human Protein Atlas

ENSG00000140557

Mus musculus

mRNA	NM_009181
Protein	NP_033207
MGI	26656

Rattus norvegicus

mRNA	NM_057156
Protein	NP_476497

FEBS Lett. 2000-06-01 ;275(24):18594-601.

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.

Angata K. et al. PMID:10766765

J. Biol. Chem. 1995-09-01 ;270(39):22685-8.

A human STX cDNA confers polysialic acid expression in mammalian cells.

Scheidegger EP. et al. PMID:7559389

DONOR : CMP-Neu5Ac

Glc	Man	Gal	GlcNAc	GalNAc	Fuc	Xyl	Neu5Ac	Neu5Gc	GlcA	IdoA	GlcN

Substrate Transferred

	JCGG-STR014102 GlyTouCan: G00065MO GlyCosmos Glycans: G00065MO	CMP-Neu5Ac	JCGG-STR033514

FEBS Lett. 1995-06-01 ;270(24):14628-33.

Molecular cloning of Sia alpha 2,3Gal beta 1,4GlcNAc alpha 2,8-sialyltransferase from mouse brain.

Yoshida Y. et al. PMID:7782326 Refer to: TABLE I

Glc	Man	Gal	GlcNAc	GalNAc	Fuc	Xyl	Neu5Ac	Neu5Gc	GlcA	IdoA	GlcN

Substrate Not Transferred

	JCGG-STR005020 GlyTouCan: G91237TK GlyCosmos Glycans: G91237TK

	JCGG-STR003473 GlyTouCan: G98544DH GlyCosmos Glycans: G98544DH

	JCGG-STR027271 GlyTouCan: G03277YI GlyCosmos Glycans: G03277YI

	JCGG-STR024659 GlyTouCan: G46677TE GlyCosmos Glycans: G46677TE

	JCGG-STR005131 GlyTouCan: G40183QN GlyCosmos Glycans: G40183QN

	JCGG-STR004466 GlyTouCan: G18625KA GlyCosmos Glycans: G18625KA

	JCGG-STR027108 GlyTouCan: G01767JJ GlyCosmos Glycans: G01767JJ

	JCGG-STR026960 GlyTouCan: G83513YI GlyCosmos Glycans: G83513YI

TABLE I Comparison of the acceptor substrate specificities of the three cloned α,8-sialyltransferases
Acceptor	Enzyme activity (pmol/ml medium/h)
Fetuin	8.0
[alpha]1-acid glycoprotein	7.6
avomucoid	1.3
bovine transferrin	0.4
BSM	0.0
Asialofetuin	0.0
lactosylceramide	0.0
Asialo-[alpha]1-acid glycoprotein	0.0

J. Biol. Chem. 1996-08-01 ;271(32):19457-63.

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.

Kojima N. et al. PMID:8702635

TABLE II Comparison of substrate glycoproteins for the sialyltransferase activity of ST8Sia II and IV
Glycoprotein	Enzyme activity (pmol/ml medium, h into 1 mg of protein)
NCAM-Fc	1590
Fetuin	2
human chrorionic gonadotropin [alpha]-subunit	1
[alpha]1-acid glycoprotein	1
human chrorionic gonadotropin beta-subunit	0

J. Biol. Chem. 1998-10-01 ;273(43):28524-32.

Differential and cooperative polysialylation of the neural cell adhesion molecule by two polysialyltransferases, PST and STX.

Angata K. et al. PMID:9774483

DONOR : CMP-Neu5Ac

Glc	Man	Gal	GlcNAc	GalNAc	Fuc	Xyl	Neu5Ac	Neu5Gc	GlcA	IdoA	GlcN

Substrate Transferred

	JCGG-STR013995 GlyTouCan: G73578JC GlyCosmos Glycans: G73578JC	CMP-Neu5Ac	JCGG-STR033515

RNA Expression from Human Protein Atlas

This RNA expression data uses "HPA data" from the Human Protein Atlas. Tissue RNA Expression

data available from v22.proteinatlas.org

J. Biol. Chem. 1995-02-01 ;360(1):1-4.

Enzymatic activity of a developmentally regulated member of the sialyltransferase family (STX): evidence for alpha 2,8-sialyltransferase activity toward N-linked oligosaccharides.

Kojima N. et al. PMID:7875291

J. Biol. Chem. 1994-07-01 ;269(27):17872-8.

Differential expression of five sialyltransferase genes in human tissues.

Kitagawa H. et al. PMID:8027041

J. Biol. Chem. 1997-03-01 ;272(11):7182-90.

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.

Angata K. et al. PMID:9054414

braincolonfetal brainfetal kidneyheartskeletal musclesmall intestinethymus

Provided by GOA

Function
alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity
sialic acid binding

Process
N-glycan processing
carbohydrate metabolic process
cellular protein modification process
ganglioside biosynthetic process
nervous system development
oligosaccharide metabolic process
protein glycosylation
sialylation

Component
Golgi membrane
early endosome
integral component of Golgi membrane
recycling endosome

ST8SIA2

Sialyltransferase

Orthologous Gene

Mus musculus

Rattus norvegicus

Acceptor Substrates (Reference)

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.

A human STX cDNA confers polysialic acid expression in mammalian cells.

DONOR : CMP-Neu5Ac

Substrate Transferred

Molecular cloning of Sia alpha 2,3Gal beta 1,4GlcNAc alpha 2,8-sialyltransferase from mouse brain.

Substrate Not Transferred

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.

Differential and cooperative polysialylation of the neural cell adhesion molecule by two polysialyltransferases, PST and STX.

DONOR : CMP-Neu5Ac

Substrate Transferred

Acceptor Substrates (KEM-C)

Expression

Expression (Reference)

Enzymatic activity of a developmentally regulated member of the sialyltransferase family (STX): evidence for alpha 2,8-sialyltransferase activity toward N-linked oligosaccharides.

Differential expression of five sialyltransferase genes in human tissues.

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.

Gene Ontology