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Information on EC 2.8.2.30 - [heparan sulfate]-glucosamine 3-sulfotransferase 3 and Organism(s) Homo sapiens and UniProt Accession Q9Y662
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2.8.2.30 [heparan sulfate]-glucosamine 3-sulfotransferase 3IUBMB Comments
Two major substrates contain the tetrasaccharides: -> undetermined 2-sulfo-uronic acid-> GlcN2S-> IdoA2S-> GlcN*-> and -> undetermined 2-sulfo-uronic acid-> GlcN2S-> IdoA2S-> GlcN6S*-> (symbols as in 2-Carb-38) with modification of the N-unsubstituted glucosamine residue (shown with an asterisk) [1,4]. Modification of selected sequences containing N-sulfo-glucosamine residues cannot yet be excluded. The 3-O-sulfated heparan sulfate can be utilized by Herpes simplex virus type 1 as an entry receptor to infect the target cells . There are two isozymes, known as 3-OST-3A and 3-OST-3B, which have identical catalytic domains but are encoded by different mammalian genes . The specificity of this enzyme differs from that of the other [heparan sulfate]-glucosamine 3-sulfotransferases. It is inefficient at modifying precursors of the antithrombin binding site [in contrast to EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1)] and it does not modify glucosamine preceded by GlcA2S [unlike EC 2.8.2.29 ([heparan sulfate]-glucosamine 3-sulfotransferase 2)].
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Word Map
- 2.8.2.30
-
3-o-sulfated
-
sulfotransferases
-
3-osts
- p120ctn
-
n-sulfated
-
hs6st1
- 3'-phosphoadenosine
-
6-o-sulfation
-
gd-binding
- octasaccharide
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antithrombin-binding
- medicine
- diagnostics
- pharmacology
- synthesis
- drug development
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
hs3st3b1, isoform 3a, hs6st3, 3-ost-3a, 3-ost-3, hs3st3a1, hs3st3b, 3-ost3a, heparan sulfate 3-o-sulfotransferase, hs3st, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-OST-3
3-OST-3A
3-OST-3B
-
-
-
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glucosaminyl 3-O-sulfotransferase 3a,3b
-
-
-
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heparan sulfate D-glucosamine 3-O-sulfotransferase 3A
-
-
-
-
heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A
heparan sulfate sulfotransferase
heparan sulfate sulfotransferase 3-OST3A
HS3ST3A
HS3ST3B
isoenzyme 3a
-
-
-
-
isoenzyme 3b
-
-
-
-
isoform 3a
-
-
-
-
isoform 3b
-
-
-
-
3-OST-3A
-
-
-
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heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A
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the enzyme generates a binding site for the envelope glycoprotein D of herpes simplex virus 1
HS3ST3A
-
-
-
-
HS3ST3B
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfate group transfer
sulfate group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase
Two major substrates contain the tetrasaccharides: -> undetermined 2-sulfo-uronic acid-> GlcN2S-> IdoA2S-> GlcN*-> and -> undetermined 2-sulfo-uronic acid-> GlcN2S-> IdoA2S-> GlcN6S*-> (symbols as in 2-Carb-38) with modification of the N-unsubstituted glucosamine residue (shown with an asterisk) [1,4]. Modification of selected sequences containing N-sulfo-glucosamine residues cannot yet be excluded. The 3-O-sulfated heparan sulfate can be utilized by Herpes simplex virus type 1 as an entry receptor to infect the target cells [2]. There are two isozymes, known as 3-OST-3A and 3-OST-3B, which have identical catalytic domains but are encoded by different mammalian genes [3]. The specificity of this enzyme differs from that of the other [heparan sulfate]-glucosamine 3-sulfotransferases. It is inefficient at modifying precursors of the antithrombin binding site [in contrast to EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1)] and it does not modify glucosamine preceded by GlcA2S [unlike EC 2.8.2.29 ([heparan sulfate]-glucosamine 3-sulfotransferase 2)].
CAS REGISTRY NUMBER
COMMENTARY
183257-54-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
3'-phosphoadenylyl sulfate + chondroitin sulfate
?
-
chondroitin sulfate exhibits similar high affinity binding to 3-OST-3A compared to heparan sulfate
-
-
?
3'-phosphoadenylyl sulfate + chondroitin sulfate A
adenosine 3',5'-diphosphate + ?
-
isoform 3A, low activity
-
?
3'-phosphoadenylyl sulfate + GlcA-beta-(1->4)-GlcNS6S-beta-(1->4)-IdoA-beta-(1->4)-GlcNS6S-alpha-(CH2)5NH2
adenosine 3',5'-bisphosphate + GlcA-beta-(1->4)-GlcNS3S6S-beta-(1->4)-IdoA-beta-(1->4)-GlcNS6S-alpha-(CH2)5NH2
-
-
-
-
?
3'-phosphoadenylyl sulfate + GlcA-beta-(1->4)-GlcNS6S-beta-(1->4)-IdoA-beta-(1->4)-GlcNS6S-beta-(1->4)-GlcA-beta-(1->4)-GlcNS6S-alpha-(CH2)5NH2
adenosine 3',5'-bisphosphate + GlcA-beta-(1->4)-GlcNS3S6S-beta-(1->4)-IdoA-beta-(1->4)-GlcNS3S6S-beta-(1->4)-GlcA-beta-(1->4)-GlcNS6S-alpha-(CH2)5NH2
-
-
-
-
?
3'-phosphoadenylyl sulfate + heparin
?
-
heparin exhibits similar high affinity binding to 3-OST-3A compared to heparan sulfate
-
-
?
3'-phosphoadenylyl sulfate + IdoA-beta-(1->4)-GlcNS6S-beta-(1->4)-IdoA-beta-(1->4)-GlcNS6S-alpha-(CH2)5NH2
adenosine 3',5'-bisphosphate + IdoA-beta-(1->4)-GlcNS3S6S-beta-(1->4)-IdoA-beta-(1->4)-GlcNS6S-alpha-(CH2)5NH2
-
-
-
-
?
3'-phosphoadenylyl sulfate + keratan sulfate
adenosine 3',5'-diphosphate + ?
-
isoform 3A, low activity
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
heparan sulfate + 3'-phosphoadenylyl sulfate
3-O-sulfated heparan sulfate + adenosine 3',5'-bisphosphate
-
i.e. PAPS
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
3-OST-3 forms IdoUA2S-AnMan3S and IdoUA2S-AnMan3S6S disaccharides-containing products, product analysis, overview
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
3-O-sulfation of GlcNH2-containing heparan sulfate by 3-OST-3 provides binding sites for glycoprotein gD of Herpes simplex virus type I and is involved in involved in cyclosporine B, CyPB, binding and viral infection, analysis of heparin sulfate structures involve, overview
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
3-OST-3 is involved in 3-OST-2-mediated HSV-1 entry into cells by catalyzing the preceeding step of 3-O-sulfated heparin sulfate modification of receptors
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
modification of the heparan sulfate of glycoprotein D gD receptors required for entry of Herpes simplex virus simplex 1, 3-OST-3 and the herpesvirus entry mediator are involved, but not nectin-1 or nectin-2, in primary croneal fibroblasts, a natural target cell type, while HeLa cells use nectin-1 as the entry receptor, overview, 3-OS HS is required for HSV-1 glycoprotein-induced cell-to-cell fusion of cultured corneal fibroblasts
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
C5 epimerization of some GlcUA into L-iduronic acid, IdoUA, 2-O-sulfation of IdoUA, and 6-O-sulfation of GlcN units
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
3-OST-3A generates a unique heparan sulfate sequence that is predicted to specifically bind envelope glycoprotein D of Herpes Simplex virus type 1, but not antithrombin III
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
isoform 3A modifies two novel tetrasaccharides of 3-O-sulfated heparan sulfate: deltaUA2S-GlcNS-IdoUA2S-S-GlcNH23S and deltaUA2S-GlcNS-IdoUA2S-3S-GlcNH23S6S
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
3-O-sulfonation of heparan sulfate by isoenzyme 3A and 3B generates binding sites for the HSV-1 glycoprotein gD and initiation of virus entry
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
isoforms 3A and 3B, isoform 3A transfers the sulfate group to IdoA2S-GlcNS, 3-O-sulfonation of glucosamine depends on the saccharide structure around the modified glucosamine residue
-
?
additional information
?
-
-
HSV-1 glycoprotein-induced cell-to-cell fusion is inhibited by either prior treatment of cells with heparinases or by heparan sulfate preparations enriched in 3-OS HS, expression of HSV-1 gD in cultured corneal fibroblasts renders resistance to HSV-1 entry, overview
-
-
?
additional information
?
-
-
binding to different glycosaminoglycans, overview
-
-
?
additional information
?
-
-
GlcA-beta-(1->4)-GlcNS6S-beta-(1->4)-GlcA-beta-(1->4)-GlcNS6S-alpha-(CH2)5NH2 and GlcA-beta-(1->4)-GlcNS6S-beta-(1->4)-IdoA2S-beta-(1->4)-GlcNS6S-alpha-(CH2)5NH2 are no substrates for isoform 3-OST-3a
-
-
?
additional information
?
-
-
isoform 3-OST3a preferentially sulfates the GlcNS6S residue when an iduronic acid residue is located to its reducing side, while 2-O-sulfation of this iduronic acid inhibits the action of isoform 3-OST3a on the target residue
-
-
?
additional information
?
-
-
isoform 3OST-3 prefers to sulfate a GlcNS(+/-)6S with an 2-O-sulfo-L-iduronic acid on the nonreducing end
-
-
?
additional information
?
-
usage of a chemoenzymatic synthetic approach to synthesize six 3-O-sulfated oligosaccharides, including three hexasaccharides and three octasaccharides. The synthesis is achieved by rearranging the enzymatic modification sequence to accommodate the substrate specificity of 3-O-sulfotransferase 3, analysis of the impact of 3-O-sulfation on the conformation of the pyranose ring of 2-O-sulfated iduronic acid using NMR spectroscopy, and on the correlation between ring conformation and anticoagulant activity. An octasaccharide interacts with antithrombin and displays anti factor Xa activity. The two 3-O-sulfotransferase (3-OST) isoforms, 3-OST-1 (EC 2.8.2.23) and 3-OST-3, are employed to install the GlcNS3S6S residue into different saccharide sequences. The 3-OST-1 enzyme introduces a sulfation to form a GlcNS3S6S residue that is linked to a GlcA residue at the nonreducing end, forming the disaccharide unit of -GlcAGlcNS3S6S-, whereas the 3-OST-3 enzyme introduces a sulfation to form a GlcNS3S residue that is linked to an IdoA2S residue at the nonreducing end, forming the disaccharide unit of -IdoA2S-GlcNS3S-. Structural and conformational analysis of oligosaccharides, overview
-
-
-
additional information
?
-
-
usage of a chemoenzymatic synthetic approach to synthesize six 3-O-sulfated oligosaccharides, including three hexasaccharides and three octasaccharides. The synthesis is achieved by rearranging the enzymatic modification sequence to accommodate the substrate specificity of 3-O-sulfotransferase 3, analysis of the impact of 3-O-sulfation on the conformation of the pyranose ring of 2-O-sulfated iduronic acid using NMR spectroscopy, and on the correlation between ring conformation and anticoagulant activity. An octasaccharide interacts with antithrombin and displays anti factor Xa activity. The two 3-O-sulfotransferase (3-OST) isoforms, 3-OST-1 (EC 2.8.2.23) and 3-OST-3, are employed to install the GlcNS3S6S residue into different saccharide sequences. The 3-OST-1 enzyme introduces a sulfation to form a GlcNS3S6S residue that is linked to a GlcA residue at the nonreducing end, forming the disaccharide unit of -GlcAGlcNS3S6S-, whereas the 3-OST-3 enzyme introduces a sulfation to form a GlcNS3S residue that is linked to an IdoA2S residue at the nonreducing end, forming the disaccharide unit of -IdoA2S-GlcNS3S-. Structural and conformational analysis of oligosaccharides, overview
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
heparan sulfate + 3'-phosphoadenylyl sulfate
3-O-sulfated heparan sulfate + adenosine 3',5'-bisphosphate
-
i.e. PAPS
-
-
?
additional information
?
-
-
HSV-1 glycoprotein-induced cell-to-cell fusion is inhibited by either prior treatment of cells with heparinases or by heparan sulfate preparations enriched in 3-OS HS, expression of HSV-1 gD in cultured corneal fibroblasts renders resistance to HSV-1 entry, overview
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
3-O-sulfation of GlcNH2-containing heparan sulfate by 3-OST-3 provides binding sites for glycoprotein gD of Herpes simplex virus type I and is involved in involved in cyclosporine B, CyPB, binding and viral infection, analysis of heparin sulfate structures involve, overview
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
3-OST-3 is involved in 3-OST-2-mediated HSV-1 entry into cells by catalyzing the preceeding step of 3-O-sulfated heparin sulfate modification of receptors
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
modification of the heparan sulfate of glycoprotein D gD receptors required for entry of Herpes simplex virus simplex 1, 3-OST-3 and the herpesvirus entry mediator are involved, but not nectin-1 or nectin-2, in primary croneal fibroblasts, a natural target cell type, while HeLa cells use nectin-1 as the entry receptor, overview, 3-OS HS is required for HSV-1 glycoprotein-induced cell-to-cell fusion of cultured corneal fibroblasts
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
isoform 3A modifies two novel tetrasaccharides of 3-O-sulfated heparan sulfate: deltaUA2S-GlcNS-IdoUA2S-S-GlcNH23S and deltaUA2S-GlcNS-IdoUA2S-3S-GlcNH23S6S
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
3-O-sulfonation of heparan sulfate by isoenzyme 3A and 3B generates binding sites for the HSV-1 glycoprotein gD and initiation of virus entry
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
isoforms 3A and 3B, isoform 3A transfers the sulfate group to IdoA2S-GlcNS, 3-O-sulfonation of glucosamine depends on the saccharide structure around the modified glucosamine residue
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-aza-2'-deoxycytidine
-
exposure of chondrosarcoma cells to the DNA-methyltransferase inhibitor 5-Aza-dc up-regulates expression of 3-OST3A mRNA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
cyclosporine B heparin binding kinetics, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
p44/42 MAPK activation, semi-quantitative expression analysis by RT-PCR, determination of unmodified heparin and cell surface binding, overview
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
primary macrophages. HS3ST3B is highly expressed in activated macrophages, highest after alternative stimulation (M2 polarization), while the enzyme is not detected in proinflammatory macrophages (M1)
HS3ST3B1 is significantly upregulated in NSCLC tissues compared with matched normal tissues. Its expression is also upregulated in mesenchymal phenotype of non-small cell lung cancer cell (NSCLC) lines compared with epithelial phenotype. When TGF-beta is applied to induce the epithelial phenotype to mesenchymal phenotype, HS3ST3B1 is upregulated compared with previous epithelial cell lines. When HS3ST3B1 is knocked down by specific small interfering RNA in the mesenchymal phenotype, mesenchymal phenotype is transformed to epithelial phenotype. HS3ST3B1 can be targeted by miR-218 in non-small cell lung cancer cells (NSCLC)
high expression level of HS3ST1 and low expression level of ZNF263
additional information
3-OST3A is epigenetically repressed in all breast cancer cell lines of a panel representative of distinct molecular subgroups, except in human epidermal growth factor receptor 2-positive (HER2+) sloan-kettering breast cancer (SKBR3) cells. Epigenetic mechanisms involved both DNA methylation and histone modifications, producing different repressive chromatin environments depending on the cell molecular signature
additional information
quantitative RT-PCR expression analysis of HS3ST3B1 in tumors and matched healthy tissues
additional information
subcellular distribution of isozymes HS3ST2 and HS3ST3B is analysed by using overexpression systems in HeLa cells
additional information
-
subcellular distribution of isozymes HS3ST2 and HS3ST3B is analysed by using overexpression systems in HeLa cells
additional information
changes in heparan sulfate sulfotransferases and cell-surface heparan sulfate occur during SKM-1 cells granulocytic differentiation and A-549 cells epithelial-mesenchymal transition. Results of RT-PCR show that ndst1, ndst2, hs2st1, hs6st1, hs6st3, hs3st3a, hs3st3b and hs3st5 mRNA are expressed during A549 cells EMT. And the other members in different sites-modifying gene families including ndst3, ndst4, hs6st2, hs3st1, hs3st2 and hs3st4 mRNA are not detected with at least two different pairs of primers and in three different PCR conditions
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
malfunction
metabolism
physiological function
additional information
evolution
both isozymes, HS3ST3B and HS3ST2 (EC 2.8.2.29), are differently expressed in monocytes and macrophages depending on the inflammatory environment
evolution
HS3STs represent the largest family of HS-modifying enzymes, and yet the reaction of 3-O-sulfation is the rarest maturation step, when compared to other sulfations. Seven HS3STs have been characterized in human, for which the expression is dependent on cell type and tissue environment
malfunction
expression of the genes encoding HS-modifying enzymes is frequently dysregulated in cancer and other diseases. The enzymes show either anti-oncogenic or tumor-promoting effects. Re-expression of HS3ST3B in MDA-MB-231 cells leads to an increase in cell viability and invasion, MDA-MB-231 cells carrying HS3ST3B expression display a significant increase in proliferation and survival. High expression of HS3ST3B in U937 leukemia cells enhances cell proliferation and survival, while its silencing has opposite effects
malfunction
HS3ST3B1 is significantly upregulated in non-small cell lung cancer cell (NSCLC) tissues compared with matched normal tissues. Its expression is also upregulated in mesenchymal phenotype of NSCLC lines compared with epithelial phenotype. When TGF-beta is applied to induce the epithelial phenotype to mesenchymal phenotype, HS3ST3B1 is upregulated compared with previous epithelial cell lines. When HS3ST3B1 is knocked down by specific small interfering RNA in the mesenchymal phenotype, mesenchymal phenotype is transformed to epithelial phenotype. HS3ST3B1 can be targeted by miR-218 in non-small cell lung cancer cells (NSCLC)
metabolism
heparan sulfate (HS) 3-O-sulfation can be catalysed by seven 3-sulfotransferases (HS3STs) in humans, but nevertheless it is the rarest modification in heparan sulfate (HS). Isozymes HS3ST2 (EC 2.8.2.29) and HS3ST3B exhibit the same activity in vitro. But they are differently expressed in macrophages depending on cell environment, which suggests that they may be involved in distinct cellular processes
metabolism
HS3ST-mediated 3-O-sulfation leads to at least two distinct forms of 3-O-sulfated motifs. HS3ST1 and HS3ST5 participate in the generation of anticoagulant-active HS/heparin sequences for antithrombin-III, while HS3ST2, HS3ST3A, HS3ST3B, HS3ST4, and HS3ST6 are described to provide the HS-binding motifs for the glycoprotein gD of herpes simplex virus-1 (HSV-1). HS3ST regulations in cancer cells, cell proliferation, and tumor progression, overview
physiological function
isoform HS3ST3B1 positively contributes to acute myeloid leukemia progression. The enzyme increases vascular endothelial growth factor expression and release by leukemia cells and promotes the activation of the Notch-1-Jagged-1, PI3K-AKT and ERK pathways
physiological function
heparan sulfate D-glucosamine 3-O-sulfotransferase 3B1 (HS3ST3B1) participates in the biosynthetic steps of heparan sulfate (HS) and targets vascular endothelial growth factor (VEGF) in acute myeloid leukemia (AML) cells, thus contributing to angiogenesis and proliferation of AML cells. HS3ST3B1 plays a role in angiogenesis and the proliferation of cancer cells. Heparan sulfate D-glucosamine 3-O-sulfotransferase 3B1 is a regulator of transforming growth factor-beta-mediated epithelial-to-mesenchymal transition and regulated by miR-218 in nonsmall cell lung cancer
physiological function
isozymes HS3ST2, HS3ST3B, and HS3ST4 may exhibit a broader selectivity. In pancreatic cancer cells, high level expression of HS3ST3B is reported to induce epithelial-mesenchymal transition (EMT) and to enhance cell invasiveness in vitro. HS3ST3B is related to an increase in the production of vascular endothelial growth factor (VEGF) and activation of downstream signalling pathways. The tumor-promoting effects of HS3ST2, HS3ST3B, and HS3ST4 are related to sustained activation of Src, Akt, and NF-kappaB, and upregulation of the anti-apoptotic proteins survivin and XIAP. Importantly, all these signalling molecules have been well described to play a critical role in promoting tumor growth and resistance to apoptosis. The tumor-promoting effect of HS3ST3B in leukemia cells is dependent on an autocrine activation of VEGF-dependent signalling pathways. HS3ST3B is described as a regulator of TGF-beta-mediated EMT in NSCLC cells. The tumor-promoting properties of HS3ST3B can be dependent on the formation of signalling complexes containing Nrp1
evolution
HS3STs represent the largest family of HS-modifying enzymes, and yet the reaction of 3-O-sulfation is the rarest maturation step, when compared to other sulfations. Seven HS3STs have been characterized in human, for which the expression is dependent on cell type and tissue environment
evolution
there are several isoforms in every gene family except that HS2ST gene family has only one isoform
malfunction
enhanced 3-O-sulfation increases binding to antithrombin, which enhances Factor Xa inhibition, and binding of neuropilin-1
malfunction
expression of the genes encoding HS-modifying enzymes is frequently dysregulated in cancer and other diseases. The enzymes show either anti-oncogenic or tumor-promoting effects. Hypermethylation in proximal regions of the HS3ST3A1 gene in chondrosarcoma. Exposure to a demethylating agent restores its expression, confirming that aberrant methylation has affected its transcription. Re-expression of HS3ST3A reduces the proliferative and migratory properties of chondrosarcoma cells, suggesting that silencing of this enzyme may have contributed to tumor cell growth and invasiveness. The HS3ST3A1 gene is epigenetically repressed in breast cancer cell lines representative of the different molecular subgroups, except in the human epidermal growth factor receptor 2-positive (HER2+) cell lines. Re-expression of the enzyme in luminal A-type MCF-7 and triple negative MDA-MB-231 cell lines reduces cell proliferation in vitro. HS3ST3A is also anti-proliferative in MDA-MB-231 cells. Overexpression of HS3ST3A does not have any effects on the proliferation of MDA-MB-231 cells
malfunction
in HER2+ patients, high level expression of 3-OST3A in tumors is associated with reduced relapse-free survival
metabolism
heparan sulfate (HS) is a type of glycosaminoglycan consisting of variably sulfated glucuronic acid or iduronic acid-Nacetylglucosamine repeating disaccharide units, and it can bind plenty of growth factors such as FGF2 and its receptor FGFR1, thereby regulating cancer cell signaling. Divergent fine structures of HS are generated by sulfation catalyzed by HS Ndeacetylase/N-, 2-O-, 6-O-, 3-O-sulfotransferases (correspondingly abbreviated as NDST, HS2ST, HS6ST, HS3ST), epimerization catalyzed by HS C5-epimerase at the Golgi lumen and further desulfation catalyzed by HS 6-O-endosulfatase at the cell surface. There are several isoforms in every gene family except that HS2ST gene family has only one isoform
metabolism
HS3ST-mediated 3-O-sulfation leads to at least two distinct forms of 3-O-sulfated motifs. HS3ST1 and HS3ST5 participate in the generation of anticoagulant-active HS/heparin sequences for antithrombin-III, while HS3ST2, HS3ST3A, HS3ST3B, HS3ST4, and HS3ST6 are described to provide the HS-binding motifs for the glycoprotein gD of herpes simplex virus-1 (HSV-1). HS3ST regulations in cancer cells, cell proliferation, and tumor progression, overview
metabolism
the sulfation at the 3-OH position of glucosamine is an important modification in forming structural domains for heparan sulfate to enable its biological functions. Seven 3-O-sulfotransferase isoforms in the human genome are involved in the biosynthesis of 3-O-sulfated heparan sulfate
metabolism
ZNF263, a C2H2 zinc finger protein, is a negative transcriptional regulator of heparin and heparan sulfate biosynthesis, which shows distinctively low expression in mast cells compared with other (non-heparin-producing) immune cells. ZNF263 is a transcriptional repressor, and its inactivation or silencing enhances mRNA expression of HS3ST1 (EC 2.8.2.23) and HS3ST3A1, enzymes involved in the formation of binding sites for antithrombin and neuropilin-1 (NRP1) and glycoprotein D of herpes simplex virus, respectively. Heparan sulfate (HS) biosynthetic genes exhibit the ZNF263 consensus motif
physiological function
-
the enzyme is a epithelial-mesenchymal transition inducer in pancreatic cancer. Overexpression of isoform 3-OST-3B1 upregulates Snail expression and triggers its nuclear translocation. The enzyme promotes in vivo angiogenic response
physiological function
-
the enzyme shows a potent inhibitory effect on hepatitis B virus replication and protein expression
physiological function
-
3-OST3A exerts dual activities acting as tumor-suppressor in MCF-7 and MDA-MB-231 cells, or as an oncogenic factor in SKBR-3 cells
physiological function
the enzyme plays a role in pre-eclampsia-associated placental dysfunction
physiological function
heparan sulfate sulfotransferase 3-OST3A (HS3ST3A) is a tumor regulator and a prognostic marker in breast cancer. Heparan sulfate (HS) proteoglycan chains are key components of the breast tumor microenvironment that critically influence the behavior of cancer cells. It is established that abnormal synthesis and processing of HS play a prominent role in tumorigenesis. HS function is mainly controlled by sulfotransferases, cellular and pathophysiological significance for the 3-O-sulfotransferase 3-OST3A (HS3ST3A), catalyzing the final maturation step of HS, in breast cancer, overview. OST3A exert dual activities acting as tumor-suppressor in lumA-michigan cancer foundation (MCF)-7 and triple negative-MD Anderson (MDA) metastatic breast (MB)-231 cells, or as an oncogenic factor in HER2+-SKBR3 cells. Mechanistically, fluorescence-resonance energy transfer-fluorescence-lifetime imaging microscopy experiments indicate that the effects of 3-OST3A in MCF-7 cells are mediated by altered interactions between HS and fibroblast growth factor-7 (FGF-7). This interplay between HS and FGF-7 modulates downstream ERK, AKT and p38 cascades, suggesting that altering 3-O-sulfation affects FGFR2IIIb-mediated signaling
physiological function
isozyme HS3ST3A may have a restricted substrate specificity, making it incapable of synthesizing 3-O-sulfated heparan sulfate (HS) with a tumor-promoting property in MDA-MB-231 cells
additional information
to date, only a few ligands are known to selectively interact with 3-O-sulfated motifs, whereas hundreds of HS-binding proteins have been identified
additional information
to date, only a few ligands are known to selectively interact with 3-O-sulfated motifs, whereas hundreds of HS-binding proteins have been identified
additional information
-
to date, only a few ligands are known to selectively interact with 3-O-sulfated motifs, whereas hundreds of HS-binding proteins have been identified
additional information
to date, only a few ligands are known to selectively interact with 3-O-sulfated motifs, whereas hundreds of HS-binding proteins have been identified
additional information
to date, only a few ligands are known to selectively interact with 3-O-sulfated motifs, whereas hundreds of HS-binding proteins have been identified
additional information
-
to date, only a few ligands are known to selectively interact with 3-O-sulfated motifs, whereas hundreds of HS-binding proteins have been identified
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HS3SB_HUMAN
390
1
43324
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
-
x * 33743, His6-tagged truncated mutant, amino acid sequence calculation, x * 33000, recombinant His6-tagged truncated mutant, SDS-PAGE
33743
-
x * 33743, His6-tagged truncated mutant, amino acid sequence calculation, x * 33000, recombinant His6-tagged truncated mutant, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
analysis of the overall structural integrity of recombinant 3-OST-3A by steady-state fluorescence spectroscopy, secondary structure with a content of 38.7% alpha-helix and 13.3% beta-sheet, overview
?
-
x * 33743, His6-tagged truncated mutant, amino acid sequence calculation, x * 33000, recombinant His6-tagged truncated mutant, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
generation of a truncated mutant enzyme depleted of its catalytic domain. The mutant shows the same localization in the Golgi as the wild-type full-length enzyme
additional information
-
generation of a truncated mutant enzyme depleted of its catalytic domain. The mutant shows the same localization in the Golgi as the wild-type full-length enzyme
additional information
-
a synthetic siRNA duplex, si3-OST-3, corresponding to 3-OST-3 mRNA sequences is used to inhibit the expression of mRNAs encoding 3-OST-3 isoforms, downregulation of the expression of 3-OST-3 by RNA interference potently reduced CyPB binding and consequent activation of p44/42 mitogen-activated protein kinases, overview
additional information
-
expression of 3-OST-3 leads to cell-to-cll fusion activity in CHO-K1 cells via gD receptors modified with 3-OS HS generated by 3-OST-3, overview
additional information
-
construction of a truncated version of 3-OST-3A starting at amino acid position G148, thereby lacking the cytoplasmic, transmembrane and SPLAG domain
additional information
generation of stable HS3STA knockdown A-549 cell line by shRNA resulting in in vitro metastasis capability of A549 cell line
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
thermal unfolding kinetics of the purified recombinant His6-tagged truncated mutant protein, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged truncated mutant isozyme 3-OST-3A lacking the cytoplasmic, transmembrane and SPLAG domain from Escherichia coli by cobalt and heparin affinity chromatography, followed by dialysis, to over 95% puritiy
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene HS3ST3B, real-time RT-PCR expression analysis, recombinant expression in HeLa cells. Analysis of subcellular localization of the recombinant isozyme
3-OST3A cDNA is inserted into the expression vector pCDNA3.1 for transfection of HEMC cells
-
expression of the N-terminally His6-tagged truncated mutant isozyme 3-OST-3A lacking the cytoplasmic, transmembrane and SPLAG domain
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the genes encoding HS-modifying enzymes is frequently dysregulated in cancer and other diseases
HS3ST3B1 is significantly upregulated in NSCLC tissues compared with matched normal tissues. Its expression is also upregulated in mesenchymal phenotype of non-small cell lung cancer cell (NSCLC) lines compared with epithelial phenotype. When TGF-beta is applied to induce the epithelial phenotype to mesenchymal phenotype, HS3ST3B1 is upregulated compared with previous epithelial cell lines
when HS3ST3B1 is knocked down by specific small interfering RNA in the mesenchymal phenotype, mesenchymal phenotype is transformed to epithelial phenotype. HS3ST3B1 can be targeted by miR-218 in non-small cell lung cancer cells (NSCLC)
3-OST3A is epigenetically repressed in all breast cancer cell lines of a panel representative of distinct molecular subgroups, except in human epidermal growth factor receptor 2-positive (HER2+) sloan-kettering breast cancer (SKBR3) cells. Epigenetic mechanisms involve both DNA methylation and histone modifications, producing different repressive chromatin environments depending on the cell molecular signature
3-OST3A is epigenetically repressed in breast cancer cell lines (except SKBR-3 cells)
-
exposure of chondrosarcoma cells to 5-aza-2'-deoxycytidine up-regulates expression of 3-OST3A mRNA
-
expression of the genes encoding HS-modifying enzymes is frequently dysregulated in cancer and other diseases
following treatment with 5-aza-2'-deoxycytidine at 24 h and both 5-aza-2'-deoxycytidine in combination with trichostatin-A at 48 h, isoform 3-OST-3B1 gene expression is activated in the pancreatic cancer cell line PANC-1
-
HS 2-O sulfotransferase 1 (HS2ST1, EC 2.8.2.) is downregulated at both mRNA and protein levels during granulocytic differentiation of SKM-1 leukemia cells and also HS (glucosamine) 3-O sulfotransferase 3A (HS3ST3A) in epithelial-mesenchymal transition (EMT) of A-549 lung cancer cells, meanwhile, cell-surface HS recognized by anti-HS antibody is also changed in both cancer cell lines. HS3ST3A is negatively correlated with the in vitro cell metastasis capability of A549 cells confirmed by RNA interference technology, wound-healing assay and in vitro Matrigel invasion assay
mRNA expression of isoform HS3ST3A1 is decreased by 27% in placental tissue obtained from preeclamptic compared to normotensive women
the enzyme is down-regulated 10fold in the hepatocytes of chronic hepatitis B virus infection model
-
the expression of isoform HS3ST3B is markedly up-regulated in human primary monocytes and the related cell line THP-1 after exposure to toll-like receptor agonists. tumor necrosis factor-alpha is also efficient, to a lesser extent, to increase isoform HS3ST3B expression, while interleukin-6, interleukin-4, and interferon-gamma are poor inducers. Lipopolysaccharide induces a rapid and strong transcription of the HS3ST3B1 gene
-
ZNF263 is a transcriptional regulator of heparin and heparan sulfate biosynthesis. CRISPR-mediated targeting and siRNA knockdown of ZNF263 in mammalian cell lines and human primary cells leads to dramatically increased expression levels of HS3ST1. LC-MS analysis of lyase-resistant 3-O-sulfated tetrasaccharides derived from ZNF263-/- cells
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
addition of 6 M guanidinium-HCl results in a red shift of the emission maximum by 12 nm indicating that the enzyme is properly folded after purification
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
medicine
pharmacology
use of a chemoenzymatic synthetic approach to synthesize six 3-O-sulfated oligosaccharides, including three hexasaccharides and three octasaccharides. The synthesis is achieved by rearranging the enzymatic modification sequence to accommodate the substrate specificity of 3-O-sulfotransferase 3, analysis of the impact of 3-O-sulfation on the conformation of the pyranose ring of 2-O-sulfated iduronic acid using NMR spectroscopy, and on the correlation between ring conformation and anticoagulant activity. An octasaccharide interacts with antithrombin and displays anti factor Xa activity. The octasaccharide displays a faster clearance rate than fondaparinux, an FDA-approved pentasaccharide drug, in a rat model, making this octasaccharide a potential short-acting anticoagulant drug candidate that could reduce bleeding risk. The presence of the -GlcNS3S6S-IdoA2S- disaccharide unit is required for anticoagulant activity
synthesis
use of a chemoenzymatic synthetic approach to synthesize six 3-O-sulfated oligosaccharides, including three hexasaccharides and three octasaccharides. The synthesis is achieved by rearranging the enzymatic modification sequence to accommodate the substrate specificity of 3-O-sulfotransferase 3, analysis of the impact of 3-O-sulfation on the conformation of the pyranose ring of 2-O-sulfated iduronic acid using NMR spectroscopy, and on the correlation between ring conformation and anticoagulant activity. An octasaccharide interacts with antithrombin and displays anti factor Xa activity. The octasaccharide displays a faster clearance rate than fondaparinux, an FDA-approved pentasaccharide drug, in a rat model, making this octasaccharide a potential short-acting anticoagulant drug candidate that could reduce bleeding risk
diagnostics
heparan sulfate sulfotransferase 3-OST3A (HS3ST3A) is a tumor regulator and a prognostic marker in breast cancer HER2+ patients for reduced relapse-free survival
diagnostics
specific HS sulfotransferases may serve as molecular markers and targets for cancer treatment
medicine
-
the results provide evidence for specific epigenetic regulation of 3-OST genes resulting in altered heparan sulfate proteoglycans and point to a defect of heparan sulfate-3-O-sulfation as a factor in cancer progression
medicine
specific HS sulfotransferases may serve as molecular markers and targets for cancer treatment
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shworak, N.W.; Liu, J.; Petros, L.M.; Zhang, L.; Kobayashi, M.; Copeland, N.G.; Jenkins, N.A.; Rosenberg, R.D.
Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase
J. Biol. Chem.
274
5170-5184
1999
Homo sapiens
Liu, J.; Shworak, N.W.; Sinay, P.; Schwartz, J.J.; Zhang, L.; Fritze, L.M.S.; Rosenberg, R.D.
Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities
J. Biol. Chem.
274
5185-5192
1999
Homo sapiens, Mus musculus
Liu, J.; Shriver, Z.; Blaiklock, P.; Yoshida, K.; Sasisekharan, R.; Rosenberg, R.D.
Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A sulfates N-unsubstituted glucosamine residues
J. Biol. Chem.
274
38155-38162
1999
Homo sapiens
Shukla, D.; Liu, J.; Blaiklock, P.; Shworak, N.W.; Bai, X.; Esko, J.D.; Cohen, G.H.; Eisenberg, R.J.; Rosenberg, R.D.; Spear, P.G.
A novel role for the 3-O-sulfated heparan sulfate in Herpes simplex virus 1 entry
Cell
99
13-22
1999
Homo sapiens, Mus musculus (Q9QZS6)
Vanpouille, C.; Deligny, A.; Delehedde, M.; Denys, A.; Melchior, A.; Lienard, X.; Lyon, M.; Mazurier, J.; Fernig, D.G.; Allain, F.
The heparin/heparan sulfate sequence that interacts with cyclophilin B contains a 3-O-sulfated N-unsubstituted glucosamine residue
J. Biol. Chem.
282
24416-24429
2007
Homo sapiens
Tiwari, V.; Clement, C.; Xu, D.; Valyi-Nagy, T.; Yue, B.Y.; Liu, J.; Shukla, D.
Role for 3-O-sulfated heparan sulfate as the receptor for herpes simplex virus type 1 entry into primary human corneal fibroblasts
J. Virol.
80
8970-8980
2006
Homo sapiens
O'Donnell, C.D.; Tiwari, V.; Oh, M.; Shukla, D.
A role for heparan sulfate 3-O-sulfotransferase isoform 2 in herpes simplex virus type 1 entry and spread
Virology
346
452-459
2006
Homo sapiens
Wille, I.; Rek, A.; Krenn, E.; Kungl, A.J.
Biophysical investigation of human heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A: a mutual effect of enzyme oligomerisation and glycosaminoglycan ligand binding
Biochim. Biophys. Acta
1774
1470-1476
2007
Homo sapiens
Bui, C.; Ouzzine, M.; Talhaoui, I.; Sharp, S.; Prydz, K.; Coughtrie, M.W.; Fournel-Gigleux, S.
Epigenetics: methylation-associated repression of heparan sulfate 3-O-sulfotransferase gene expression contributes to the invasive phenotype of H-EMC-SS chondrosarcoma cells
FASEB J.
24
436-450
2010
Homo sapiens
Song, K.; Li, Q.; Jiang, Z.Z.; Guo, C.W.; Li, P.
Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3B1, a novel epithelial-mesenchymal transition inducer in pancreatic cancer
Cancer Biol. Ther.
12
388-398
2011
Homo sapiens
Liu, J.; Moon, A.; Sheng, J.; Pedersen, L.
Understanding the substrate specificity of the heparan sulfate sulfotransferases by an integrated biosynthetic and crystallographic approach
Curr. Opin. Struct. Biol.
22
550-557
2012
Homo sapiens
Nguyen, T.K.; Arungundram, S.; Tran, V.M.; Raman, K.; Al-Mafraji, K.; Venot, A.; Boons, G.J.; Kuberan, B.
A synthetic heparan sulfate oligosaccharide library reveals the novel enzymatic action of D-glucosaminyl 3-O-sulfotransferase-3a
Mol. Biosyst.
8
609-614
2012
Homo sapiens
Zhang, Z.; Liu, X.; Chen, J.; Su, H.; Luo, Q.; Ye, J.; Tang, N.; Zhang, W.; Chen, W.; Ko, B.C.; Huang, A.
Heparin sulphate D-glucosaminyl 3-O-sulfotransferase 3B1 plays a role in HBV replication
Virology
406
280-285
2010
Homo sapiens
Zhang, L.; Song, K.; Zhou, L.; Xie, Z.; Zhou, P.; Zhao, Y.; Han, Y.; Xu, X.; Li, P.
Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3B1 (HS3ST3B1) promotes angiogenesis and proliferation by induction of VEGF in acute myeloid leukemia cells
J. Cell. Biochem.
116
1101-1112
2015
Homo sapiens (Q9Y662)
Sikora, A.S.; Delos, M.; Martinez, P.; Carpentier, M.; Allain, F.; Denys, A.
Regulation of the expression of heparan sulfate 3-O-sulfotransferase 3B (HS3ST3B) by inflammatory stimuli in human monocytes
J. Cell. Biochem.
117
1529-1542
2016
Homo sapiens
Thacker, B.E.; Xu, D.; Lawrence, R.; Esko, J.D.
Heparan sulfate 3-O-sulfation: a rare modification in search of a function
Matrix Biol.
35
60-72
2014
Homo sapiens (Q9Y663)
Mao, X.; Gauche, C.; Coughtrie, M.W.; Bui, C.; Gulberti, S.; Merhi-Soussi, F.; Ramalanjaona, N.; Bertin-Jung, I.; Diot, A.; Dumas, D.; De Freitas Caires, N.; Thompson, A.M.; Bourdon, J.C.; Ouzzine, M.; Fournel-Gigleux, S.
The heparan sulfate sulfotransferase 3-OST3A (HS3ST3A) is a novel tumor regulator and a prognostic marker in breast cancer
Oncogene
35
5043-5055
2016
Homo sapiens
Amraoui, F.; Hassani Lahsinoui, H.; Boussata, S.; Keijser, R.; Veenboer, G.J.; Middeldorp, S.; van der Post, J.A.; Ris-Stalpers, C.; Afink, G.B.; van den Born, B.J.
Placental expression of heparan sulfate 3-O-sulfotransferase-3A1 in normotensive and pre-eclamptic pregnancies
Placenta
36
1218-1224
2015
Homo sapiens (Q9Y663), Homo sapiens
Delos, M.; Foulquier, F.; Hellec, C.; Vicogne, D.; Fifre, A.; Carpentier, M.; Papy-Garcia, D.; Allain, F.; Denys, A.
Heparan sulfate 3-O-sulfotransferase 2 (HS3ST2) displays an unexpected subcellular localization in the plasma membrane
Biochim. Biophys. Acta
1862
1644-1655
2018
Homo sapiens (Q9Y662), Homo sapiens
Denys, A.; Allain, F.
The emerging roles of heparan sulfate 3-O-sulfotransferases in cancer
Front. Oncol.
9
507
2019
Homo sapiens (Q9Y662), Homo sapiens (Q9Y663), Homo sapiens
Zhao, S.; Wang, Z.
Changes in heparan sulfate sulfotransferases and cell-surface heparan sulfate during SKM-1 cells granulocytic differentiation and A549 cells epithelial-mesenchymal transition
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37
151-164
2020
Homo sapiens (Q9Y663)
Wang, Z.; Hsieh, P.H.; Xu, Y.; Thieker, D.; Chai, E.J.E.; Xie, S.; Cooley, B.; Woods, R.J.; Chi, L.; Liu, J.
Synthesis of 3-O-sulfated oligosaccharides to understand the relationship between structures and functions of heparan sulfate
J. Am. Chem. Soc.
139
5249-5256
2017
Homo sapiens (Q9Y663), Homo sapiens
Zhang, Z.; Jiang, H.; Wang, Y.; Shi, M.
Heparan sulfate D-glucosamine 3-O-sulfotransferase 3B1 is a novel regulator of transforming growth factor-beta-mediated epithelial-to-mesenchymal transition and regulated by miR-218 in nonsmall cell lung cancer
J. Cancer Res. Ther.
14
24-29
2018
Homo sapiens (Q9Y662)
Mao, X.; Gauche, C.; Coughtrie, M.W.; Bui, C.; Gulberti, S.; Merhi-Soussi, F.; Ramalanjaona, N.; Bertin-Jung, I.; Diot, A.; Dumas, D.; De Freitas Caires, N.; Thompson, A.M.; Bourdon, J.C.; Ouzzine, M.; Fournel-Gigleux, S.
The heparan sulfate sulfotransferase 3-OST3A (HS3ST3A) is a novel tumor regulator and a prognostic marker in breast cancer
Oncogene
35
5043-5055
2016
Homo sapiens (Q9Y663), Homo sapiens
Weiss, R.J.; Spahn, P.N.; Toledo, A.G.; Chiang, A.W.T.; Kellman, B.P.; Li, J.; Benner, C.; Glass, C.K.; Gordts, P.L.S.M.; Lewis, N.E.; Esko, J.D.
ZNF263 is a transcriptional regulator of heparin and heparan sulfate biosynthesis
Proc. Natl. Acad. Sci. USA
117
9311-9317
2020
Homo sapiens (Q9Y663), Homo sapiens
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