Any feedback?
No. of entries
Information on EC 2.4.1.174 - glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase
for references in articles please use BRENDA:EC2.4.1.174
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.174 glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase
IUBMB Comments
Requires Mn2+. Involved in the biosynthesis of chondroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
The enzyme appears in viruses and cellular organisms
- 2.4.1.174
- glycosaminoglycans
- proteoglycans
- aggrecan
- laxity
-
perineuronal
Reaction Schemes
showSynonyms
csgalnact1, csgalnact2, chondroitin sulfate n-acetylgalactosaminyltransferase 1, galnact-ii, chondroitin n-acetylgalactosaminyltransferase-1, chondroitin sulfate n-acetylgalactosaminyltransferase 2, n-acetylgalactosaminet-ii, galnact-i, chondroitin beta1,4-n-acetylgalactosaminyltransferase-1, chondroitin n-acetylgalactosaminyltransferase-2, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-chondroitin, I
-
-
-
-
ChGn-1
ChGn-2
chondroitin galactosaminyltransferase
chondroitin N-acetylgalactosaminyltransferase-1
chondroitin N-acetylgalactosaminyltransferase-2
chondroitin sulfate beta-1,4-N-acetylgalactosaminyltransferase-1 ChGn-1
-
chondroitin sulfate N-acetylgalactosaminyltransferase 1
chondroitin sulfate N-acetylgalactosaminyltransferase 2
chondroitin sulfate N-acetylgalactosaminyltransferase-1
chondroitin sulfate N-acetylgalactosaminyltransferase-2
CS N-acetylgalactosaminyltransferase 1
CSGalNAcT-1
CSGalNAcT1
CSGALNACT2
GalNAcT-I
GalNAcT-II
glucuronylgalactosylproteoglycan beta-1,4-N-acetylgalactosaminyltransferase
-
-
-
-
N-acetylgalactosaminyltransferase I
-
-
-
-
uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase I
-
-
-
-
additional information
chondroitin sulfate N-acetylgalactosaminyltransferase 1
-
additional information
the enzyme has also N-acetylgalactosaminyltransferase II activity, EC 2.4.1.175, substrates sulfated and unsulfated chondroitin oligo- and polysaccharides
additional information
the enzyme has also N-acetylgalactosaminyltransferase II activity, EC 2.4.1.175, substrates chondroitin oligo- and polysaccharides
additional information
the enzyme has also N-acetylgalactosaminyltransferase II activity, EC 2.4.1.175, substrates chondroitin oligo- and polysaccharides
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-galactosamine + [protein]-3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine = UDP + [protein]-3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine
UDP-N-acetyl-alpha-D-galactosamine + [protein]-3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine = UDP + [protein]-3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine
-
-
-
-
UDP-N-acetyl-alpha-D-galactosamine + [protein]-3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine = UDP + [protein]-3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine
the enzyme mainly regulates CS synthesis in cartilage
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
chondroitin biosynthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-galactosamine:D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase
Requires Mn2+. Involved in the biosynthesis of chondroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
96189-39-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactose
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactose
-
Substrates: minimum requirement for acceptor structure
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactose
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactose
-
Substrates: best substrate
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-(Gly)Ser-(Gly-Glu)
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-(Gly)Ser-(Gly-Glu)
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-Ser
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-Ser
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-Ser-peptide
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-Ser-peptide
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,4-beta-D-glucose
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,4-beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
UDP-N-acetyl-D-galactosamine + GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
UDP + N-acetyl-D-galactosaminyl-1-4beta-D-GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
UDP-N-acetyl-D-galactosamine + GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin
UDP + N-acetyl-D-galactosaminyl-1-4beta-D-GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
E7F6G2, A8E7C8
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
Substrates: i.e. linkage tetrasaccharide, synthetic substrate
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
Substrates: best acceptor substrate together with chondroitin polysaccharide
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
Substrates: transfers GalNAc to GlcA at the non-reducing terminus of the linkage tetrasacharide
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
UDP + N-acetyl-D-galactosaminyl-1-4beta-D-GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
Substrates: a phosphorylated tetrasaccharide linkage structure in ChGn-1-/- growth plate cartilage but not in ChGn-2-/- or wild-type growth plate cartilage, preferred substrate of ChGn-1
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
UDP + N-acetyl-D-galactosaminyl-1-4beta-D-GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
Substrates: a phosphorylated tetrasaccharide linkage structure in ChGn-1-/- growth plate cartilage but not in ChGn-2-/- or wild-type growth plate cartilage, preferred substrate of ChGn-1
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin
UDP + N-acetyl-D-galactosaminyl-1-4beta-D-GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin
UDP + N-acetyl-D-galactosaminyl-1-4beta-D-GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
-
Substrates: acceptors are tri- or disaccharides with terminal glucuronyl residue and a galactosyl residue in penultimate position, transfers acetylgalactosamine in beta-linkage, no substrates are glucuronic acid or disaccharides with terminal galactosyl residues
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
-
Substrates: involved in chondroitin sulfate biosynthesis: transfer of the first N-acetylgalactosamine residue
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
-
Substrates: involved in the biosynthesis of chodroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
Substrates: involved in chondroitin initiation and elongation
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
Substrates: involved in the biosynthesis of chodroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
Products: -
Products: -
?
additional information
?
-
-
Substrates: GalNAcT activity of the recombinant enzyme is determined using a trisaccharide analogue of the linkage region linked to a chromophoric aglycone, GlcA-beta1,3-Gal-beta1,3-Gal-O-methoxyphenyl, i.e. GlcA-Gal-Gal-OMP, as a acceptor substrate, Km is 3.8 mM, and with only the trisaccharide GlcA-beta1,3-Gal-beta1,3-Gal, Km 3.39 mM, no activity with Gal-Gal-OMP. The enzyme activity is even higher with 4- and 6-sulfated GlcA-Gal-Gal-OMP, kM values are 0.6 mM and 1.0 mm, respectively, no activity with 6-disulfated GlcA-Gal-Gal-OMP
Products: -
Products: -
?
additional information
?
-
-
Substrates: in vitro chondroitin polymerization does not occur on the non-reducing terminal GalNAc-linkage pentasaccharide structure
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin and GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin and GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin and GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin and GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
additional information
?
-
-
Substrates: in vitro chondroitin polymerization does not occur on the non-reducing terminal GalNAc-linkage pentasaccharide structure
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
E7F6G2, A8E7C8
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
-
Substrates: involved in chondroitin sulfate biosynthesis: transfer of the first N-acetylgalactosamine residue
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
-
Substrates: involved in the biosynthesis of chodroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
Substrates: involved in chondroitin initiation and elongation
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
Substrates: involved in the biosynthesis of chodroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(E)-2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-(2-phenylprop-1-enyl)benzoic acid
-
(E)-2-hydroxy-4-methoxy-3-prenyl-6-(2-(thiophen-2-yl)vinyl)-benzoic acid
-
(E)-3-(3,7-dimethylocta-2,6-dienyl)-2-hydroxy-4-methoxy-6-phenethylbenzoic acid
-
(E)-isopropyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzoate
-
(E)-methyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-(2-phenylprop-1-enyl)benzoate
-
(E)-methyl 2-hydroxy-4-methoxy-3-prenyl-6-(2-(thiophen-2-yl)-vinyl)benzoate
-
(E)-methyl 6-(4-(tert-butyldimethylsilyloxy)styryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-N-cyclopropyl-2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzamide
-
(E)-tert-butyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzoate
-
2-hydroxy-4-methoxy-3-prenyl-6-((1E,3E)-4-phenylbuta-1,3-dienyl)benzoic acid
-
cajanine
cajanine is a stilbenic component isolated from Cajanus cajan, it is identified as a potent hepatitis C virus (HCV) inhibitor by phenotypic screening with EC50 of 0.00317 mM. Cajanine inhibits HCV infection by targeting cellular CSGalNAcT-1 protein destabilizing the protein. Cajanine does not inhibit HCV replication at the replicative steps of HCV life cycle. CSGalNAcT-1 is important to support HCV replication at the early stage. Structure-activity relationships and the mechanism of action, and analysis of cajanine derivatives, EC50 values, overview. Cajanine might inhibit HCV replication at early steps of the viral life cycle via downregulating of cellular CSGalNAcT-1
methyl 2-hydroxy-4-methoxy-3-prenyl-6-((1E,3E)-4-phenylbuta-1,3-dienyl)benzoate
-
additional information
2-hydroxy-4-methoxy-6-[(E)-2-phenylethenyl]benzoic acid is not inhibitory
-
additional information
heparan sulfate-synthesis enzymes inhibits chondroitin sulfate as extracellular inhibitor of axon growth
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinogenesis
Glycosyltransferase expression in human colonic tissue examined by oligonucleotide arrays.
Carcinoma
Glycosylation is an Androgen-Regulated Process Essential for Prostate Cancer Cell Viability.
Hepatitis C
Design and Synthesis of Cajanine Analogues against Hepatitis C Virus through Down-Regulating Host Chondroitin Sulfate N-Acetylgalactosaminyltransferase 1.
Hereditary Sensory and Motor Neuropathy
Chondroitin beta-1,4-N-acetylgalactosaminyltransferase-1 missense mutations are associated with neuropathies.
Infections
Chondroitin sulfate N-acetylgalactosaminyltransferase-2 contributes to the replication of infectious bursal disease virus via interaction with the capsid protein VP2.
Intervertebral Disc Degeneration
Upregulation of glycosaminoglycan synthesis by Neurotropin in nucleus pulposus cells via stimulation of chondroitin sulfate N-acetylgalactosaminyltransferase 1: A new approach to attenuation of intervertebral disc degeneration.
Joint Instability
Chondroitin Sulfate N-acetylgalactosaminylTransferase-1 (CSGalNAcT-1) Deficiency Results in a Mild Skeletal Dysplasia and Joint Laxity.
Kashin-Beck Disease
Abnormal expression of chondroitin sulphate N-acetylgalactosaminyltransferase 1 and Hapln-1 in cartilage with Kashin-Beck disease and primary osteoarthritis.
Language Development Disorders
CSGALNACT1-congenital disorder of glycosylation: A mild skeletal dysplasia with advanced bone age.
Neoplasm Metastasis
Glycosyltransferase expression in human colonic tissue examined by oligonucleotide arrays.
Neoplasms
Polymorphisms Within the RET Proto-Oncogene and Risk of Sporadic Medullary Thyroid Carcinoma.
Osteoarthritis
Abnormal expression of chondroitin sulphate N-acetylgalactosaminyltransferase 1 and Hapln-1 in cartilage with Kashin-Beck disease and primary osteoarthritis.
Polyneuropathies
Chondroitin beta-1,4-N-acetylgalactosaminyltransferase-1 missense mutations are associated with neuropathies.
Prostatic Neoplasms
Glycosylation is a global target for androgen control in prostate cancer cells.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
transfected cells are injected into the cuadal intervertebral discs of 4-month old ICR mice, analyses at day seven after the injection show, that in vivo gene delivery of chondroitin sulfate N-acetylgalactosaminyltransferase-1 increases chondroitin sulfate biosynthesis in cartilage.
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expression of Chsy1 is up-regulated in skeletal elements
brenda
additional information
quantitative gene expression and in situ hybridization of genes associated with endochondral ossification
brenda
-
quantitative gene expression and in situ hybridization of genes associated with endochondral ossification
-
brenda
-
quantitative analysis of Csgalnact1 and Csgalnact2 transcripts in brain of wild-type and Csgalnact1-/- mice by real-time PCR, overview
brenda
-
quantitative analysis of Csgalnact1 and Csgalnact2 transcripts in brain of wild-type and Csgalnact1-/- mice by real-time PCR, overview
-
brenda
knee, quantitative RT-PCR enzyme expression analysis of CSGALNACT1
brenda
knee, quantitative RT-PCR enzyme expression analysis of CSGALNACT2
brenda
-
knee, quantitative RT-PCR enzyme expression analysis of CSGALNACT1
-
brenda
-
knee, quantitative RT-PCR enzyme expression analysis of CSGALNACT2
-
brenda
additional information
gene csgalnact1 expression analysis during fish development, in situ immunohistochemic analysis, overview. Gene csgalnact1 mRNA is not maternally deposited, instead a rather weak and ubiquitous expression is seen during early somitogenesis. At 24 hr post fertilization, gene csgalnact1 expression is mostly restricted to the notochord and to the otic capsule, but weak staining is also seen in the intermediate cell mass, a hematopoietic region at this stage. At later stages, csgalnact1 expression becomes restricted mainly to cartilage structures, and the regions of the pharyngeal arches, the otic capsule, the pectoral fins, the notochord, and the median fin fold. At 72 hr post fertilization, weak staining in brain tissue and the spinal cord appears, while strong staining is detected in cartilage structures and the brain ventricular zone
brenda
additional information
A8E7C8
gene csgalnact1 expression analysis during fish development, in situ immunohistochemic analysis, overview. Gene csgalnact1 mRNA is not maternally deposited, instead a rather weak and ubiquitous expression is seen during early somitogenesis. At 24 hr post fertilization, gene csgalnact1 expression is mostly restricted to the notochord and to the otic capsule, but weak staining is also seen in the intermediate cell mass, a hematopoietic region at this stage. At later stages, csgalnact1 expression becomes restricted mainly to cartilage structures, and the regions of the pharyngeal arches, the otic capsule, the pectoral fins, the notochord, and the median fin fold. At 72 hr post fertilization, weak staining in brain tissue and the spinal cord appears, while strong staining is detected in cartilage structures and the brain ventricular zone
brenda
additional information
gene csgalnact2 expression analysis during fish development, in situ immunohistochemic analysis, overview. The csgalnact2 probe strongly stains embryos already at the 2-cell stage indicating maternally deposited mRNA. Notochord staining is visible already from the 5-somite stage and expression is apparent at the 15-somite stage in the tail bud and in the notochord, whereas the expression at 24 hr post fertilization is restricted to the brain tissue and the posterior region of the somites and the notochord. Expression is further detected in brain tissue at 36 and 48 hr post fertilization when staining appeared also in the pectoral fins, the notochord, the otic capsule, and cartilage structures. By 72 hr post fertilization, expression is restricted to the head, the spinal cord, and the pronephric ducts
brenda
additional information
A8E7C8
gene csgalnact2 expression analysis during fish development, in situ immunohistochemic analysis, overview. The csgalnact2 probe strongly stains embryos already at the 2-cell stage indicating maternally deposited mRNA. Notochord staining is visible already from the 5-somite stage and expression is apparent at the 15-somite stage in the tail bud and in the notochord, whereas the expression at 24 hr post fertilization is restricted to the brain tissue and the posterior region of the somites and the notochord. Expression is further detected in brain tissue at 36 and 48 hr post fertilization when staining appeared also in the pectoral fins, the notochord, the otic capsule, and cartilage structures. By 72 hr post fertilization, expression is restricted to the head, the spinal cord, and the pronephric ducts
brenda
additional information
immunohistochemic analysis of enzyme content and localization, overview
brenda
additional information
isozymes CSGALNACT1 (T1) and CSGALNACT2 (T2) are expressed in different organs
brenda
additional information
isozymes CSGALNACT1 (T1) and CSGALNACT2 (T2) are expressed in different organs
brenda
additional information
-
the enzyme is expressed (at very high levels) in the prehypertrophic zone of the growth plate at E16.5, colocalized with aggrecan core protein. In ATDC5 cells the expression of CSGlcAT and CSGalNAcT-1 correlate well with that of aggrecan core protein. Real time RT-PCR show a high level of chondroitin sulfate N-acetylgalactosaminyltransferase-1 expression in cartilage at E18.5.
brenda
additional information
-
CSS1 quantitative tissue expression analysis by realtime RT-PCR, overview
brenda
additional information
isozymes CSGALNACT1 (T1) and CSGALNACT2 (T2) are expressed in different organs
brenda
additional information
isozymes CSGALNACT1 (T1) and CSGALNACT2 (T2) are expressed in different organs
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
confocal microscopy analysis of isozyme localization
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
evolution
E7F6G2, A8E7C8
the CSGALNACT1 and CSGALNACT2 isozymes enzymes both have a GT7 catalytic domain with beta(1->4)-N-acetylgalactosaminyl transferase
malfunction
metabolism
physiological function
additional information
drug target
the enzyme (ChGn-2) may serve as a promising target for direct vessel wall therapy
malfunction
missense mutations are found in gene ChGn-1 in exon 5, H234R, and exon 10, M509R, respectively, in two patients with neuropathy. The mutations might be associated with the pathogenetic mechanisms of the peripheral neuropathies
malfunction
-
CSS2 knockout chondrocyte culture systems, together with siRNA of CSS1, reveal the presence of two CS chain species in length, suggesting two steps of CS chain polymerization; i.e., elongation from the linkage region up to Mr of about 10000 and further extension
malfunction
-
deficiency in chondroitin N-acetylgalactosaminyltransferase-1 reduces the numbers of chondroitin sulfate chains, leading to skeletal dysplasias in mice. Knockdown of ChGn-1 decreases chondroitin sulfate levels in L cells, chondroitin sulfate chain lengths in L-shRNAChGn-1-1, L-shRNA ChGn-1-2, and mock-transfected murine L cells, overview
malfunction
-
chondroitin sulfate production is reduced by approximately half in CSGalNAcT1-null mice, and the amount of short-chain CS is also reduced compared to wild-type mice. CSGalNAcT1-null mice have reduced skeletal growth, thickness of the growth plate is reduced, and the cartilage of the null mice is significantly smaller than that of wild-type mice, phenotype, overview
malfunction
-
Chsy1-/- mice show a profound limb patterning defect in which orthogonally shifted ectopic joints form in the distal digits. Associated with the digit-patterning defect is a shift in cell orientation and an imbalance in chondroitin sulfation. Chondrogenesis is impaired as early as E13.5 in Chsy1-/- embryos. Ectopic, split digit phenotype, overview
malfunction
-
the growth plate of Csgalnact1-/- mice contains shorter and slightly disorganized chondrocyte columns with a reduced volume of the extracellular matrix principally in the proliferative layer. Immunohistochemical analysis reveals that the level of both aggrecan and link protein 1 are decreased in Csgalnact1-/- cartilage with an increase in processed forms of aggrecan core protein, phenotype, overview
malfunction
mice carrying a gene knockout for chondroitin sufate N-acetylgalactosaminyltransferase-1, mutant T1KO, recover more completely from spinal cord injury than wild-type mice and even chondroitinase ABC-treated mice. Synthesis of heparan sulfate, a glycosaminoglycan promoting axonal growth, is also upregulated in TI knockout mice because heparan sulfate-synthesis enzymes are induced in the mutant neurons. Chondroitinase ABC treatment never induces heparan sulfate upregulation. T1KO mice are viable, but they have abnormal bone development and 10% shorter bodies compared to wild-type mice. Reduced chondroitin sulfate levels are associated with reduced scar formation in T1KO mice. Phenotype of enzyme knockout mutant mice, overview
malfunction
the enzyme is downregulated in Kashin-Beck disease (KBD), an endemic degenerative osteoarthritis, and in primary osteoarthritis, both associated with extracellular matrix degradation. Enzyme CSGalNAcT-1 may be involved in the damage of articular cartilage of Kashin-Beck disease and osteoarthritis by regulating Hapln-1 in the Wnt/beta-catenin signalling pathway. Alterations of involved enzyme expressions in CSGalNAcT gene network in case of Kashin-Beck disease and osteoarthritis
malfunction
deficiency in chondroitin N-acetylgalactosaminyltransferase-1 reduces the number of chondroitin sulfate chains, leading to skeletal dysplasias in mice. Accumulation of phosphorylated pentasaccharide and tetrasaccharide linkages in ChGn-1-/- growth plate cartilage
malfunction
knockdown of CSGalNAcT2 inhibits infectious bursal disease virus replication involving the integrity of the Golgi apparatus
malfunction
T1KO mice show microscopic abnormalities in the CNS, but are fertile and viable. They have 10% smaller body sizes than wild-type mice due to abnormal skeletal development
malfunction
after silencing of endogenous CSGalNAcT-1 with specific siRNA, the intracellular hepatitis C virus (HCV) RNA load is largely reduced, and the HCV core protein is declined as well
malfunction
saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core CS synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1). rVAR2 inhibits cellular migration, invasion, and anchorage independent growth in cancer. rVAR2 interacts with chondroitin sulfate glycosaminoglycan (ofCS)-modified proteoglycans
malfunction
saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core chondroitin sulfate (CS) synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1). rVAR2 inhibits cellular migration, invasion, and anchorage independent growth in cancer. rVAR2 interacts with chondroitin sulfate glycosaminoglycan (ofCS)-modified proteoglycans
malfunction
t1 single knockout mice (t1 KO) exhibit slight dwarfism and a reduction in chondroitin sulfate (CS) content in cartilage compared with wild-type mice. Impaired chondroitin sulfate (CS) content in cartilage and induction of abnormal endochondral ossification is caused by t1::t2 (CSGALNACT1/CSGALNACT2) double deficiency. DKO mice exhibit postnatal lethality. Col2-DKO mice survive to adulthood and show severe dwarfism compared with t1 KO mice. Histological analysis of epiphyseal cartilage from Col2-DKO mice reveals disrupted endochondral ossification, characterized by drastic GAG reduction in the extracellular matrix. DKO cartilage has reduced chondrocyte proliferation and an increased number of apoptotic chondrocytes compared with wild-type cartilage. Conversely, primary chondrocyte cultures from Col2-DKO knee cartilage have the same proliferation rate as wild-type chondrocytes and low GAG expression levels, indicating that the chondrocytes themselves have an intact proliferative ability. Quantitative RT-PCR analysis of E18.5 cartilage shows that the expression levels of Col2a1 and Ptch1 transcripts tend to decrease in DKO compared with those in wild-type mice. The CS content in DKO cartilage is decreased compared with that in t1 KO cartilage
malfunction
impaired chndroitin sulfate (CS) content in cartilage and induction of abnormal endochondral ossification is caused by t1::t2 (CSGALNACT1/CSGALNACT2) double deficiency. DKO mice exhibit postnatal lethality, whereas t2 KO mice show normal size and skeletal development. Col2-DKO mice survive to adulthood and show severe dwarfism. Histological analysis of epiphyseal cartilage from Col2-DKO mice reveals disrupted endochondral ossification, characterized by drastic GAG reduction in the extracellular matrix. DKO cartilage has reduced chondrocyte proliferation and an increased number of apoptotic chondrocytes compared with wild-type cartilage. Conversely, primary chondrocyte cultures from Col2-DKO knee cartilage have the same proliferation rate as wild-type chondrocytes and low GAG expression levels, indicating that the chondrocytes themselves have an intact proliferative ability. Quantitative RT-PCR analysis of E18.5 cartilage shows that the expression levels of Col2a1 and Ptch1 transcripts tend to decrease in DKO compared with those in wild-type mice. Phenotype of t2 null mice, overview
malfunction
chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1) deficiency results in a mild skeletal dysplasia and joint laxity
malfunction
abnormalities in perineuronal nets and behavior are observed in mice lacking CSGalNAcT1. Loss of this enzyme reduces the amount of chondroitin sulfate (CS) by approximately 50% in various brain regions. The amount of CS in perineuronal nets (PNNs) is also diminished in T1KO compared to wild-type mice, although the amount of a major CS proteoglycan core protein, aggrecan, is not changed. In T1KO, abnormalities in several behavioral tests, including the open-field test, acoustic startle response, and social preference are observed. Phenotype, overview
malfunction
ChGn-2-deficient mice show decreased and shortened glycosaminoglycans. Deletion of the enzyme reduces macrophage foam cell formation and mice atherosclerosis
malfunction
chondroitin sulfate N-acetylgalactosyltransferase-1 knockout shows milder phenotype in experimental autoimmune encephalomyelitis than in wild type
malfunction
deletion of chondroitin sulfate N-acetylgalactosaminyltransferase 2 reduces macrophage foam cell formation and mice atherosclerosis. ChGn-2-deficient mice show decreased and shortened glycosaminoglycans
malfunction
-
the growth plate of Csgalnact1-/- mice contains shorter and slightly disorganized chondrocyte columns with a reduced volume of the extracellular matrix principally in the proliferative layer. Immunohistochemical analysis reveals that the level of both aggrecan and link protein 1 are decreased in Csgalnact1-/- cartilage with an increase in processed forms of aggrecan core protein, phenotype, overview
-
malfunction
-
deficiency in chondroitin N-acetylgalactosaminyltransferase-1 reduces the number of chondroitin sulfate chains, leading to skeletal dysplasias in mice. Accumulation of phosphorylated pentasaccharide and tetrasaccharide linkages in ChGn-1-/- growth plate cartilage
-
malfunction
-
saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core chondroitin sulfate (CS) synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1). rVAR2 inhibits cellular migration, invasion, and anchorage independent growth in cancer. rVAR2 interacts with chondroitin sulfate glycosaminoglycan (ofCS)-modified proteoglycans
-
malfunction
-
t1 single knockout mice (t1 KO) exhibit slight dwarfism and a reduction in chondroitin sulfate (CS) content in cartilage compared with wild-type mice. Impaired chondroitin sulfate (CS) content in cartilage and induction of abnormal endochondral ossification is caused by t1::t2 (CSGALNACT1/CSGALNACT2) double deficiency. DKO mice exhibit postnatal lethality. Col2-DKO mice survive to adulthood and show severe dwarfism compared with t1 KO mice. Histological analysis of epiphyseal cartilage from Col2-DKO mice reveals disrupted endochondral ossification, characterized by drastic GAG reduction in the extracellular matrix. DKO cartilage has reduced chondrocyte proliferation and an increased number of apoptotic chondrocytes compared with wild-type cartilage. Conversely, primary chondrocyte cultures from Col2-DKO knee cartilage have the same proliferation rate as wild-type chondrocytes and low GAG expression levels, indicating that the chondrocytes themselves have an intact proliferative ability. Quantitative RT-PCR analysis of E18.5 cartilage shows that the expression levels of Col2a1 and Ptch1 transcripts tend to decrease in DKO compared with those in wild-type mice. The CS content in DKO cartilage is decreased compared with that in t1 KO cartilage
-
malfunction
-
impaired chndroitin sulfate (CS) content in cartilage and induction of abnormal endochondral ossification is caused by t1::t2 (CSGALNACT1/CSGALNACT2) double deficiency. DKO mice exhibit postnatal lethality, whereas t2 KO mice show normal size and skeletal development. Col2-DKO mice survive to adulthood and show severe dwarfism. Histological analysis of epiphyseal cartilage from Col2-DKO mice reveals disrupted endochondral ossification, characterized by drastic GAG reduction in the extracellular matrix. DKO cartilage has reduced chondrocyte proliferation and an increased number of apoptotic chondrocytes compared with wild-type cartilage. Conversely, primary chondrocyte cultures from Col2-DKO knee cartilage have the same proliferation rate as wild-type chondrocytes and low GAG expression levels, indicating that the chondrocytes themselves have an intact proliferative ability. Quantitative RT-PCR analysis of E18.5 cartilage shows that the expression levels of Col2a1 and Ptch1 transcripts tend to decrease in DKO compared with those in wild-type mice. Phenotype of t2 null mice, overview
-
malfunction
-
chondroitin sulfate production is reduced by approximately half in CSGalNAcT1-null mice, and the amount of short-chain CS is also reduced compared to wild-type mice. CSGalNAcT1-null mice have reduced skeletal growth, thickness of the growth plate is reduced, and the cartilage of the null mice is significantly smaller than that of wild-type mice, phenotype, overview
-
metabolism
-
CSS1 and CSS2 differently contribute to chondroitin sulfate biosynthesis, mechanism of chondroitin sulfate biosynthesis, overview. CSS1 participates in both the chondroitin sulfate chain initiation and polymerization, and CSS2 participates in the polymerization, especially in further extension
metabolism
-
chondroitin sulfate biosynthetic pathway and relevant glycosyltransferases, overview
metabolism
E7F6G2, A8E7C8
the enzyme belongs to the zebrafish CS/DS glycosyltransferases are spatially and temporally expressed. Ooverlapping expression of multiple glycosyltransferases coincides with high CS/DS deposition. Efficient CS/DS biosynthesis requires a combination of several glycosyltransferases
metabolism
E7F6G2, A8E7C8
the enzyme belongs to the zebrafish CS/DS glycosyltransferases are spatially and temporally expressed. Overlapping expression of multiple glycosyltransferases coincides with high CS/DS deposition. Efficient CS/DS biosynthesis requires a combination of several glycosyltransferases
metabolism
chondroitin sulfate N-acetylgalactosaminyl-transferase-1 is a key enzyme in chondroitin sulfate biosynthesis
metabolism
the first step (GalNAc transfer) of chondroitin sulfate (CS) backbone synthesis is performed by at least two isoforms, CSGALNACT1 (T1) and CSGALNACT2 (T2), which are expressed in different organs, CS metabolism, roles of CS and perineuronal nets (PNNs) in brain function from the perspective of CS synthesis, overview
metabolism
the first step (GalNAc transfer) of chondroitin sulfate (CS) backbone synthesis is performed by at least two isoforms, CSGALNACT1 (T1) and CSGALNACT2 (T2), which are expressed in different organs, CS metabolism, roles of CS and perineuronal nets (PNNs) in brain function from the perspective of CS synthesis, overview
metabolism
six glycosyltransferases are known to coordinately synthesize the backbone structure of chondroitin sulfate (CS). Two glycosyltransferases, Csgalnact1 (t1) and Csgalnact2 (t2), are critical for initiation of CS synthesis in vitro. According to an in vitro enzymatic characterization, among the six CS glycosyltransferases, only t1 and t2 possessed the ability to independently initiate CS synthesis. t1 efficiently transfers GalNAc onto the linkage tetrasaccharide in vitro, which is common to both CS and heparin sulfate/heparin, and t1 initiation activity is stronger than that of t2
metabolism
CSGalNAcT-1 plays a role in chondroitin sulfate and dermatan sulfate synthesis
metabolism
CSGalNAcT1 is a key enzyme in chondroitin sulfate synthesis. Chondroitin sulfate (CS) is an important glycosaminoglycan and is mainly found in the extracellular matrix as CS proteoglycans. In the brain, CS proteoglycans are highly concentrated in perineuronal nets (PNNs), which surround synapses and modulate their functions
metabolism
-
chondroitin sulfate biosynthetic pathway and relevant glycosyltransferases, overview
-
metabolism
-
six glycosyltransferases are known to coordinately synthesize the backbone structure of chondroitin sulfate (CS). Two glycosyltransferases, Csgalnact1 (t1) and Csgalnact2 (t2), are critical for initiation of CS synthesis in vitro. According to an in vitro enzymatic characterization, among the six CS glycosyltransferases, only t1 and t2 possessed the ability to independently initiate CS synthesis. t1 efficiently transfers GalNAc onto the linkage tetrasaccharide in vitro, which is common to both CS and heparin sulfate/heparin, and t1 initiation activity is stronger than that of t2
-
physiological function
-
ChGn-1 initiates chondroitin sulfate biosynthesis by transferring the first N-acetylgalactosamine to the tetrasaccharide in the protein linkage region of chondroitin sulfate, overview. c-2 efficiently transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate to position 4 of non-reducing terminal GalNAc-linkage residues, and the number of chondroitin chains is regulated by the expression levels of C4ST-2 and of ChGn-1. C4ST-2 plays a key role in regulating levels of chondroitin sulfate synthesized via ChGn-1, overview
physiological function
-
chondroitin sulfate N-acetylgalactosaminyltransferase-1 is required for normal cartilage development
physiological function
-
Chsy1 catalyzes the extension of chondroitin and dermatan sulfate glycosaminoglycans and is an essential regulator of joint patterning
physiological function
-
chondroitin sulfate N-acetylgalactosaminyltransferase-1, CSGalNAcT-1, is involved in chondroitin sulfate initiation, but not in elongation
physiological function
-
chondroitin sulfate N-acetylgalactosaminyltransferase 1, CSGalNAcT-1, participates in the chondroitin sulfate chain initiation and is necessary for normal endochondral ossification and aggrecan metabolism
physiological function
E7F6G2, A8E7C8
the enzyme is involved in chondroitin sulfate biosynthesis. Chondroitin/dermatan sulfate (CS/DS) proteoglycans present in the extracellular matrix have important structural and regulatory functions. The CSGALNACT1 and CSGALNACT2 isozymes initiate CS/DS formation by the addition of a GalNAc residue to a proteoglycan tetrasaccharide linkage region attached to a core protein, but may also participate in the later steps of CS/DS polymerization
physiological function
E7F6G2, A8E7C8
the enzyme is involved in chondroitin sulfate biosynthesis. Chondroitin/dermatan sulfate (CS/DS) proteoglycans present in the extracellular matrix have important structural and regulatory functions. CS/DS is a ubiquitous component of multicellular organisms with mechanical functions in cartilage, but also is required for fundamental processes such as cell division and cytokinesis. The CSGALNACT1 and CSGALNACT2 isozymes initiate CS/DS formation by the addition of a GalNAc residue to a proteoglycan tetrasaccharide linkage region attached to a core protein, but may also participate in the later steps of CS/DS polymerization
physiological function
ChGn-1 is a key enzyme for production of chondroitin sulfate proteoglycans The clinical course of multiple sclerosis is influenced by the level of expression of the ChGn-1 gene. Chondroitin sulfate proteoglycans are a constituent of the matrix of the central nervous system (CNS), likely participating as regulatory molecules in the process of demyelination, remyelination, axonaldegeneration and regeneration in the CNS
physiological function
chondroitin sulfate N-acetylgalactosaminyl-transferase-1 is an essential enzyme in chondroitin sulfate metabolism and participates in chondroitin sulfate chain formation of aggrecan, and plays an important role in degenerative extracellular matrix of cartilage
physiological function
chondroitin N-acetylgalactosaminyltransferase-1 regulates the number of chondroitin sulfate chains for normal cartilage development. ChGn-1-mediated addition of N-acetylgalactosamine is accompanied by rapid 2-phosphoxylose phosphatase XYLP-dependent dephosphorylation during formation of the CS linkage region. ChGn-1 and XYLP cooperatively regulate the number of chondroitin sulfate chains in growth plate cartilage
physiological function
chondroitin sulfate N-acetylgalactosaminyltransferase-2 contributes to the replication of infectious bursal disease virus, IBDV, via interaction with capsid protein VP2. Overexpression of CSGalNAcT2 promotes IBDV replication in DF1 cells involving the integrity of the Golgi apparatus
physiological function
chondroitin sulfate N-acetylgalactosaminyltransferase 1 initiates synthesis of chondroitin sulfate side chains attached to a core protein of aggrecan, which is a predominant disc matrix component
physiological function
CSGalNAcT-1 is essential for hepatitis C virus (HCV) replication in human cells
physiological function
the enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) are key players in the core chondroitin sulfate (CS) synthesis. Oncofetal chondroitin sulfate glycosaminoglycans (ofCSs) are key players in integrin signaling and tumor cell motility, overview
physiological function
enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) are key players in the core chondroitin sulfate (CS) synthesis. Oncofetal chondroitin sulfate glycosaminoglycans (ofCSs) are key players in integrin signaling and tumor cell motility, overview
physiological function
both chondroitin sulfate N-acetylgalactosaminyltransferase 1 (t1) and chondroitin sulfate N-acetylgalactosaminyltransferase 2 (t2) are necessary for chondroitin sulfate (CS) synthesis and normal chondrocyte differentiation but are not sufficient for all CS synthesis in cartilage. CS biosynthesis is initiated by the transfer of GalNAc residues to the linkage region, which consists of tetrasaccharide units of GlcUA-beta1,3-galactose (Gal)-beta1,3-Gal-beta1,4-xylose (Xyl) attached to the serine residues of the core proteins. This triggers CS elongation by alternating addition of GalNAc and GlcUA residues, which is catalyzed by six glycosyltransferases in mammals. Enzyme t1 and t2 are known to function in both initiation and elongation activity. t1 exhibits stronger initiation activity than t2, indicating that t1 has a vital role in CS synthesis initiation
physiological function
both chondroitin sulfate N-acetylgalactosaminyltransferase 1 (t1) and chondroitin sulfate N-acetylgalactosaminyltransferase 2 (t2) are necessary for chondroitin sulfate (CS) synthesis and normal chondrocyte differentiation but are not sufficient for all CS synthesis in cartilage. CS biosynthesis is initiated by the transfer of GalNAc residues to the linkage region, which consists of tetrasaccharide units of GlcUA-beta1,3-galactose (Gal)-beta1,3-Gal-beta1,4-xylose (Xyl) attached to the serine residues of the core proteins. This triggers CS elongation by alternating addition of GalNAc and GlcUA residues, which is catalyzed by six glycosyltransferases in mammals. t1 and t2 are known to function in both initiation and elongation activity. Enzyme t1 exhibits stronger initiation activity than t2, indicating that t1 has a vital role in CS synthesis initiation
physiological function
CSGALNACT1 encodes chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1, ChGn-1), which initiates chondroitin sulfate (CS) chain biosynthesis on the so-called GAG-protein linker region tetrasaccharide
physiological function
enzyme CSGalNAcT1 is important for plasticity, probably due to regulation of CS-dependent perineuronal nets (PNNs). It plays an important role in supplying CS for PNN development and brain functions related to several characteristic behaviors
physiological function
the enzyme impacts foam cell formation and atherosclerosis by altering macrophage glycosaminoglycan chain. The enzyme (ChGn-2) enables oxidized low-density lipoprotein binding on the macrophage surface
physiological function
foam cell formation is significantly altered by ChGn-2 in both mouse peritoneal macrophages and the RAW264.7 macrophage cell line. Mechanistically, ChGn-2 enhances oxidized low-density lipoprotein binding on the cell surface, and as a consequence, CD36 (an important macrophage membrane scavenger receptor) is differentially regulated
physiological function
-
chondroitin sulfate N-acetylgalactosaminyltransferase 1, CSGalNAcT-1, participates in the chondroitin sulfate chain initiation and is necessary for normal endochondral ossification and aggrecan metabolism
-
physiological function
-
chondroitin N-acetylgalactosaminyltransferase-1 regulates the number of chondroitin sulfate chains for normal cartilage development. ChGn-1-mediated addition of N-acetylgalactosamine is accompanied by rapid 2-phosphoxylose phosphatase XYLP-dependent dephosphorylation during formation of the CS linkage region. ChGn-1 and XYLP cooperatively regulate the number of chondroitin sulfate chains in growth plate cartilage
-
physiological function
-
enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) are key players in the core chondroitin sulfate (CS) synthesis. Oncofetal chondroitin sulfate glycosaminoglycans (ofCSs) are key players in integrin signaling and tumor cell motility, overview
-
physiological function
-
both chondroitin sulfate N-acetylgalactosaminyltransferase 1 (t1) and chondroitin sulfate N-acetylgalactosaminyltransferase 2 (t2) are necessary for chondroitin sulfate (CS) synthesis and normal chondrocyte differentiation but are not sufficient for all CS synthesis in cartilage. CS biosynthesis is initiated by the transfer of GalNAc residues to the linkage region, which consists of tetrasaccharide units of GlcUA-beta1,3-galactose (Gal)-beta1,3-Gal-beta1,4-xylose (Xyl) attached to the serine residues of the core proteins. This triggers CS elongation by alternating addition of GalNAc and GlcUA residues, which is catalyzed by six glycosyltransferases in mammals. Enzyme t1 and t2 are known to function in both initiation and elongation activity. t1 exhibits stronger initiation activity than t2, indicating that t1 has a vital role in CS synthesis initiation
-
physiological function
-
both chondroitin sulfate N-acetylgalactosaminyltransferase 1 (t1) and chondroitin sulfate N-acetylgalactosaminyltransferase 2 (t2) are necessary for chondroitin sulfate (CS) synthesis and normal chondrocyte differentiation but are not sufficient for all CS synthesis in cartilage. CS biosynthesis is initiated by the transfer of GalNAc residues to the linkage region, which consists of tetrasaccharide units of GlcUA-beta1,3-galactose (Gal)-beta1,3-Gal-beta1,4-xylose (Xyl) attached to the serine residues of the core proteins. This triggers CS elongation by alternating addition of GalNAc and GlcUA residues, which is catalyzed by six glycosyltransferases in mammals. t1 and t2 are known to function in both initiation and elongation activity. Enzyme t1 exhibits stronger initiation activity than t2, indicating that t1 has a vital role in CS synthesis initiation
-
physiological function
-
chondroitin sulfate N-acetylgalactosaminyltransferase-1 is required for normal cartilage development
-
additional information
-
the enzyme occurs in a heterooligomer complex, chondroitin sulfate synthase-1 (CSS1)/chondroitin synthase-1
additional information
proportion of linkage region saccharides from wild-type, ChGn-1-/-, or ChGn-2-/- cartilage, overview
additional information
proportion of linkage region saccharides from wild-type, ChGn-1-/-, or ChGn-2-/- cartilage, overview
additional information
quantitative analysis of six CS glycosyltransferase transcripts using real-time RT-PCR
additional information
quantitative analysis of six CS glycosyltransferase transcripts using real-time RT-PCR
additional information
-
proportion of linkage region saccharides from wild-type, ChGn-1-/-, or ChGn-2-/- cartilage, overview
-
additional information
-
quantitative analysis of six CS glycosyltransferase transcripts using real-time RT-PCR
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). CHSSA_CAEEL
736
1
83557
Swiss-Prot
other Location (Reliability: 1)
CGAT2_HUMAN
542
1
62572
Swiss-Prot
other Location (Reliability: 3)
E1C2T4_CHICK
540
0
62294
TrEMBL
Mitochondrion (Reliability: 3)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70000
x * 70000, about, recombinant His-tagged soluble forms of wild-type ChGn-1 and S126LChGn-1 mutant enzymes, SDS-PAGE
95000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 70000, about, recombinant His-tagged soluble forms of wild-type ChGn-1 and S126LChGn-1 mutant enzymes, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
2 potential N-glycosylation sites, either one or both of which are used in COS-1 cells during expression of the recombinant fusion protein
glycoprotein
2 potential N-glycosylation sites, either one or both of which are used in COS-1 cells during expression of the recombinant fusion protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H234R
naturally occuring mutation in exon 5 of gene ChGn1, the mutant shows neuropathy, Bells palsy and/or hereditary motor and sensory neuropathy, the mutant enzyme is inactive
M509R
naturally occuring mutation in exon 10 of gene ChGn1, the mutant shows neuropathy, Bells palsy and/or hereditary motor and sensory neuropathy, the mutant enzyme is inactive
additional information
additional information
overexpression and siRNA-mediated knockdown of gene CSGalNAcT2 in DF1 cells
additional information
-
overexpression and siRNA-mediated knockdown of gene CSGalNAcT2 in DF1 cells
additional information
saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core chondroitin sulfate (CS) synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) via siRNA. The oncofetal chondroitin sulfate glycosaminoglycans (ofCS) modification is highly expressed in both human and murine metastatic lesions in situ and pre-incubation or early intravenous treatment of tumor cells with rVAR2-inhibited seeding and spreading of tumor cells in mice
additional information
-
saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core chondroitin sulfate (CS) synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) via siRNA. The oncofetal chondroitin sulfate glycosaminoglycans (ofCS) modification is highly expressed in both human and murine metastatic lesions in situ and pre-incubation or early intravenous treatment of tumor cells with rVAR2-inhibited seeding and spreading of tumor cells in mice
additional information
bi-allelic loss-of-function mutations in CSGALNACT1 produce a skeletal dysplasia reminiscent of the skeletal dysplasia of Csgalnact1-/- mice, and adds to the genetic heterogeneity of Desbuquois dysplasia (DD)
additional information
-
bi-allelic loss-of-function mutations in CSGALNACT1 produce a skeletal dysplasia reminiscent of the skeletal dysplasia of Csgalnact1-/- mice, and adds to the genetic heterogeneity of Desbuquois dysplasia (DD)
additional information
-
in cmd mice (known as natural aggrecan-null mice) the heterozygote and homozygote cartilage exhibit about 50% and about 9% aggrecan gene transcription respectively. In the cmd heterozygote cartilage, chondroitin sulfate N-acetylgalactosaminyltransferase-1 expression is dimnished to about 30% that of the wild type. In the cmd homozygote cartilage, chondroitin sulfate N-acetylgalactosaminyltransferase-1 expression furhter decreases to a low level.
additional information
-
construction of L-shRNA ChGn-1-1 and L-shRNA ChGn-1-2 transfected L cells, and analysis of chondroitin sulfate chain lengths. The silencing of the genes results in a 60-80% reduction in steady-state ChGn-1 mRNA and an 18-22% decrease in CS when compared with control L cells. Overexpression of ChGn-1 slightly increases CS levels in L cells
additional information
-
construction of CSGalNAcT1-null mice by homologous recombination using an embryonic stem cell line, RENKA, developed from the wild-type C57BL/6N strain
additional information
-
generation of Csgalnact1-/- mice by using a targeting vector for Csgalnact1 gene disruption
additional information
construction of RNAi-mediated gene Csgalnact1 knockout mice, mutant T1KO. T1KO mice are viable, but they have abnormal bone development and 10% shorter bodies compared to wild-type mice. Heparan sulfate synthesis increases in injured spinal cords of T1KO mice
additional information
saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core CS synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) via siRNA. The oncofetal chondroitin sulfate glycosaminoglycan chains (ofCS) modification is highly expressed in both human and murine metastatic lesions in situ and pre-incubation or early intravenous treatment of tumor cells with rVAR2-inhibited seeding and spreading of tumor cells in mice
additional information
-
saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core CS synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) via siRNA. The oncofetal chondroitin sulfate glycosaminoglycan chains (ofCS) modification is highly expressed in both human and murine metastatic lesions in situ and pre-incubation or early intravenous treatment of tumor cells with rVAR2-inhibited seeding and spreading of tumor cells in mice
additional information
generation of single knockout T1 KO mutant and of double knockout mutant Col2-DKO, a chondrocyte-specific t1::t2 KO mutant, quantitative RT-PCR analysis of knee cartilage shows no or slight t1 and t2 gene expression in Col2-DKO mice compared with wild-type mice. t1::t2 double KO mice show severe dwarfism and postnatal lethality, pgenotype, overview
additional information
generation of single knockout T1 KO mutant and of double knockout mutant Col2-DKO, a chondrocyte-specific t1::t2 KO mutant, quantitative RT-PCR analysis of knee cartilage shows no or slight t1 and t2 gene expression in Col2-DKO mice compared with wild-type mice. t1::t2 double KO mice show severe dwarfism and postnatal lethality, pgenotype, overview
additional information
generation of single knockout T2 KO mutant and of double knockout mutant Col2-DKO, a chondrocyte-specific t1::t2 KO mutant, quantitative RT-PCR analysis of knee cartilage shows no or slight t1 and t2 gene expression in Col2-DKO mice compared with wild-type mice. t1::t2 double KO mice show severe dwarfism and postnatal lethality, phenotype, overview
additional information
generation of single knockout T2 KO mutant and of double knockout mutant Col2-DKO, a chondrocyte-specific t1::t2 KO mutant, quantitative RT-PCR analysis of knee cartilage shows no or slight t1 and t2 gene expression in Col2-DKO mice compared with wild-type mice. t1::t2 double KO mice show severe dwarfism and postnatal lethality, phenotype, overview
additional information
generation of mice that are deficient in the CS synthesizing enzyme, CSGalNAcT1 (T1KO)
additional information
-
generation of Csgalnact1-/- mice by using a targeting vector for Csgalnact1 gene disruption
-
additional information
-
saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core CS synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) via siRNA. The oncofetal chondroitin sulfate glycosaminoglycan chains (ofCS) modification is highly expressed in both human and murine metastatic lesions in situ and pre-incubation or early intravenous treatment of tumor cells with rVAR2-inhibited seeding and spreading of tumor cells in mice
-
additional information
-
generation of single knockout T1 KO mutant and of double knockout mutant Col2-DKO, a chondrocyte-specific t1::t2 KO mutant, quantitative RT-PCR analysis of knee cartilage shows no or slight t1 and t2 gene expression in Col2-DKO mice compared with wild-type mice. t1::t2 double KO mice show severe dwarfism and postnatal lethality, pgenotype, overview
-
additional information
-
generation of single knockout T2 KO mutant and of double knockout mutant Col2-DKO, a chondrocyte-specific t1::t2 KO mutant, quantitative RT-PCR analysis of knee cartilage shows no or slight t1 and t2 gene expression in Col2-DKO mice compared with wild-type mice. t1::t2 double KO mice show severe dwarfism and postnatal lethality, phenotype, overview
-
additional information
-
construction of CSGalNAcT1-null mice by homologous recombination using an embryonic stem cell line, RENKA, developed from the wild-type C57BL/6N strain
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially solubilized with a buffer containing 2% Triton X-100, 20% glycerol and phospholipase A2
-
recombinant His-tagged soluble forms of wild-type ChGn-1 and S126LChGn-1 mutant from COS-1 cellsby nickel affinity chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, expression of a truncated form, consisting of the putative catalytic domain, in Spodoptera frugiperda Sf21 insect cells as a soluble FLAG-tagged protein
DNA sequence determination, genomic organization and chromosome localization, functional expression as soluble protein fused to protein A IgG-binding domain in COS-1 cells, secretion into the medium
gene ChGn1, expression of His-tagged wild-type ChGn-1 and soluble mutant enzymes in COS-1 cells, secretion to the medium
gene CSGALNACT1 or t1, quantitative RT-PCR enzyme expression analysis of CS glycosyltransferases
gene csgalnact1, DNA and amino acid sequence determination and analysis, phylogenetic analysis
E7F6G2, A8E7C8
gene CSGALNACT1, genotyping and polymorphisms, recombinant expression of His-tagged soluble forms of wild-type ChGn-1 and S126LChGn-1 mutant in COS-1 cells, the enzymes are secreted
gene CSGALNACT1, quantitative real-time PCR enzyme expression analysis
gene CSGALNACT1, quantitative real-time RT-PCR enzyme expression analysis
gene CSGalNAcT1, recombinant expression of wild-type and mutant FLAG-tagged CSGalNAcT-1 enzymes in COS-7 cells
gene CSGALNACT2 or t2, quantitative RT-PCR enzyme expression analysis of CS glycosyltransferases
gene CSGalNAcT2, cloning from DF-1 cells, overexpression in DF1 cells, semiquantitative real-time RT-PCR enzyme expression analysis, interaction analysis of enzyme CSGalNAcT2 with IBDV viral capsid protein VP2using the yeast two-hybridization assay
gene csgalnact2, DNA and amino acid sequence determination and analysis, phylogenetic analysis
E7F6G2, A8E7C8
gene CSGALNACT2, quantitative real-time RT-PCR enzyme expression analysis
LTC cells from rat chondrosarcoma are transfected with chondroitin sulfate N-acetylgalactosaminyltransferase-1 expression plasmid (about 80fold increase of chondroitin sulfate N-acetylgalactosaminyltransferase-1 RNA), metabolic albeling with [35S]sulfate show up to a 2.2fold increase in chondroitin sulfate levels in these cells, but the mRNA level of aggrecan core protein does not change. Aggrecan obained from chondroitin sulfate N-acetylgalactosaminyltransferase-1 overexpressing cells contain a larger amount of chondroitin sulfate, but the chondroitin sulfate chain length is similar to mock-transfected cells.
-
DNA sequence determination, genomic organization and chromosome localization, functional expression as soluble protein fused to protein A IgG-binding domain in COS-1 cells, secretion into the medium
DNA sequence determination, genomic organization and chromosome localization, functional expression as soluble protein fused to protein A IgG-binding domain in COS-1 cells, secretion into the medium
gene CSGALNACT1, quantitative real-time PCR enzyme expression analysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cajanine is a stilbenic component isolated from Cajanus cajan, it is identified as a potent hepatitis C virus (HCV) inhibitor by phenotypic screening with EC50 of 0.00317 mM. Cajanine inhibits HCV infection by targeting cellular CSGalNAcT-1 protein destabilizing the protein. Cajanine does not inhibit HCV replication at the replicative steps of HCV life cycle. CSGalNAcT-1 is important to support HCV replication at the early stage. Structure-activity relationships and the mechanism of action, and analysis of cajanine derivatives, overview. Cajanine might inhibit HCV replication at early steps of the viral life cycle via downregulating of cellular CSGalNAcT-1
CSGalNAcT2 gene expression is upregulated during infectious bursal disease virus, IBDV, infection
enzyme expression is induced by Neutropin (NTP). Neurotropin activates the phosphatidylinositol 3-kinase-AKT pathway and AKT stimulation, it stimulate glycosaminoglycan synthesis through upregulation of expression of mRNA for chondroitin sulfate N-acetylgalactosaminyltransferase 1. Gene expression profiling shows over 2fold upregulation of 697 genes in response to Neurotropin treatment. Upregulation of IGF1, ANG1, and CSGALNACT1 expression by NTP. Neurotropin (NTP) is a nonprotein extract from inflamed rabbit skin inoculated with vaccinia virus, it has been widely used in Japan and China as an analgesic drug for treatment of chronic pain, such as LBP, postherpetic neuralgia, neck-shoulder-arm syndrome, hyperesthesia of subacute myelo-optic neuropathy, and fibromyalgia. Addition of NTP to the culture medium of nucleus pulposus cells enhances proteoglycan synthesis to halt progressive intervertebral disc (IVD) degeneration
in macrophages ChGn-2 expression is upregulated in the presence of oxidized low-density lipoproteins
in macrophages, ChGn-2 expression is upregulated in the presence of oxLDL (oxidized LDL)
induction of gene CSGalNAcT-2 by NTP is much lower compared to CSGalNAcT-1
T1 is upregulated in reactive astrocytes after spinal cord injury (SCI)
the enzyme is downregulated in Kashin-Beck disease (KBD), an endemic degenerative osteoarthritis, and in primary osteoarthritis, both associated with extracellular matrix degradation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
the enzyme is an anti-HCV target to combat drug resistance. Cajanine derivatives are a class of anti-HCV agents downregulating the enzyme
drug development
functional link of oncofetal chondroitin sulfate glycosaminoglycan chains (ofCS) modifications with cancer cell motility, chondroitin sulfate synthesis knockdown is a therapeutic cancer target
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rohrmann, K.; Niemann, R.; Buddecke, E.
Two N-acetylgalactosaminyltransferases are involved in the biosynthesis of chondroitin sulfate
Eur. J. Biochem.
148
463-469
1985
Bos taurus
brenda
Gotoh, M.; Sato, T.; Akashima, T.; Iwasaki, H.; Kameyama, A.; Mochizuki, H.; Yada, T.; Inaba, N.; Zhang, Y.; Kikuchi, N.; Kwon, Y.D.; Togayachi, A.; Kudo, T.; Nishihara, S.; Watanabe, H.; Kimata, K.; Narimatsu, H.
Enzymatic synthesis of chondroitin with a novel chondroitin sulfate N-acetylgalactosaminyltransferase that transfers N-acetylgalactosamine to glucuronic acid in initiation and elongation of chondroitin sulfate synthesis
J. Biol. Chem.
277
38189-38196
2002
Homo sapiens (Q8TDX6)
brenda
Uyama, T.; Kitagawa, H.; Tamura, J.I.; Sugahara, K.
Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase. The key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate
J. Biol. Chem.
277
8841-8846
2002
Homo sapiens (Q8TDX6)
brenda
Uyama, T.; Kitagawa, H.; Tanaka, J.; Tamura, J.i.; Ogawa, T.; Sugahara, K.
Molecular cloning and expression of a second chondroitin N-acetylgalactosaminyltransferase involved in the initiation and elongation of chondroitin/dermatan sulfate
J. Biol. Chem.
278
3072-3078
2003
Homo sapiens (Q8TDX6), Homo sapiens (Q8N6G5)
brenda
Sakai, K.; Kimata, K.; Sato, T.; Gotoh, M.; Narimatsu, H.; Shinomiya, K.; Watanabe, H.
Chondroitin sulfate N-acetylgalactosaminyltransferase-1 plays a critical role in chondroitin sulfate synthesis in cartilage
J. Biol. Chem.
282
4152-4161
2007
Homo sapiens, Mus musculus
brenda
Watanabe, Y.; Takeuchi, K.; Higa Onaga, S.; Sato, M.; Tsujita, M.; Abe, M.; Natsume, R.; Li, M.; Furuichi, T.; Saeki, M.; Izumikawa, T.; Hasegawa, A.; Yokoyama, M.; Ikegawa, S.; Sakimura, K.; Amizuka, N.; Kitagawa, H.; Igarashi, M.
Chondroitin sulfate N-acetylgalactosaminyltransferase-1 is required for normal cartilage development
Biochem. J.
432
47-55
2010
Mus musculus, Mus musculus C57BL/6N
brenda
Izumikawa, T.; Koike, T.; Kitagawa, H.
Chondroitin 4-O-sulfotransferase-2 regulates the number of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1
Biochem. J.
441
697-705
2012
Mus musculus
brenda
Wilson, D.G.; Phamluong, K.; Lin, W.Y.; Barck, K.; Carano, R.A.; Diehl, L.; Peterson, A.S.; Martin, F.; Solloway, M.J.
Chondroitin sulfate synthase 1 (Chsy1) is required for bone development and digit patterning
Dev. Biol.
363
413-425
2012
Mus musculus
brenda
Gulberti, S.; Jacquinet, J.C.; Chabel, M.; Ramalanjaona, N.; Magdalou, J.; Netter, P.; Coughtrie, M.W.; Ouzzine, M.; Fournel-Gigleux, S.
Chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1) involved in chondroitin sulfate initiation: impact of sulfation on activity and specificity
Glycobiology
22
561-571
2012
Homo sapiens
brenda
Sato, T.; Kudo, T.; Ikehara, Y.; Ogawa, H.; Hirano, T.; Kiyohara, K.; Hagiwara, K.; Togayachi, A.; Ema, M.; Takahashi, S.; Kimata, K.; Watanabe, H.; Narimatsu, H.
Chondroitin sulfate N-acetylgalactosaminyltransferase 1 is necessary for normal endochondral ossification and aggrecan metabolism
J. Biol. Chem.
286
5803-5812
2011
Mus musculus, Mus musculus C57/BL6J
brenda
Saigoh, K.; Izumikawa, T.; Koike, T.; Shimizu, J.; Kitagawa, H.; Kusunoki, S.
Chondroitin beta-1,4-N-acetylgalactosaminyltransferase-1 missense mutations are associated with neuropathies
J. Hum. Genet.
56
143-146
2011
Homo sapiens (Q8TDX6), Homo sapiens
brenda
Ogawa, H.; Hatano, S.; Sugiura, N.; Nagai, N.; Sato, T.; Shimizu, K.; Kimata, K.; Narimatsu, H.; Watanabe, H.
Chondroitin sulfate synthase-2 is necessary for chain extension of chondroitin sulfate but not critical for skeletal development
PLoS ONE
7
e43806
2012
Mus musculus
brenda
Filipek-Gorniok, B.; Holmborn, K.; Haitina, T.; Habicher, J.; Oliveira, M.B.; Hellgren, C.; Eriksson, I.; Kjellen, L.; Kreuger, J.; Ledin, J.
Expression of chondroitin/dermatan sulfate glycosyltransferases during early zebrafish development
Dev. Dyn.
242
964-975
2013
Danio rerio (E7F6G2), Danio rerio (A8E7C8)
brenda
Zheng, J.; Wu, C.; Ma, W.; Zhang, Y.; Hou, T.; Xu, H.; Wu, S.; Yao, X.; Guo, X.
Abnormal expression of chondroitin sulphate N-acetylgalactosaminyltransferase 1 and Hapln-1 in cartilage with Kashin-Beck disease and primary osteoarthritis
Int. Orthop.
37
2051-2059
2013
Homo sapiens (Q8TDX6)
brenda
Izumikawa, T.; Sato, B.; Mikami, T.; Tamura, J.; Igarashi, M.; Kitagawa, H.
GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate) is the preferred substrate for chondroitin N-acetylgalactosaminyltransferase-1
J. Biol. Chem.
290
5438-5448
2015
Mus musculus (Q8BJQ9), Mus musculus (Q8C1F4), Mus musculus C57BL/6 (Q8BJQ9), Mus musculus C57BL/6 (Q8C1F4)
brenda
Takeuchi, K.; Yoshioka, N.; Higa Onaga, S.; Watanabe, Y.; Miyata, S.; Wada, Y.; Kudo, C.; Okada, M.; Ohko, K.; Oda, K.; Sato, T.; Yokoyama, M.; Matsushita, N.; Nakamura, M.; Okano, H.; Sakimura, K.; Kawano, H.; Kitagawa, H.; Igarashi, M.
Chondroitin sulphate N-acetylgalactosaminyl-transferase-1 inhibits recovery from neural injury
Nat. Commun.
4
2740
2013
Mus musculus (Q8BJQ9)
brenda
Saigoh, K.; Yoshimura, S.; Izumikawa, T.; Miyata, S.; Tabara, Y.; Matsushita, T.; Miki, T.; Miyamoto, K.; Hirano, M.; Kitagawa, H.; Kira, J.I.; Kusunoki, S.
Chondroitin sulfate beta-1,4-N-acetylgalactosaminyltransferase-1 (ChGn-1) polymorphism: association with progression of multiple sclerosis
Neurosci. Res.
108
55-59
2016
Homo sapiens (Q8TDX6)
brenda
Zhang, L.; Ren, X.; Chen, Y.; Gao, Y.; Wang, N.; Lu, Z.; Gao, L.; Qin, L.; Wang, Y.; Gao, H.; Li, K.; Jiang, L.; Cui, H.; Liu, C.; Zhang, Y.; Qi, X.; Wang, X.
Chondroitin sulfate N-acetylgalactosaminyltransferase-2 contributes to the replication of infectious bursal disease virus via interaction with the capsid protein VP2
Viruses
7
1474-1491
2015
Gallus gallus (E1C2T4), Gallus gallus
brenda
Vodopiutz, J.; Mizumoto, S.; Lausch, E.; Rossi, A.; Unger, S.; Janocha, N.; Costantini, R.; Seidl, R.; Greber-Platzer, S.; Yamada, S.; Mueller, T.; Jilma, B.; Ganger, R.; Superti-Furga, A.; Ikegawa, S.; Sugahara, K.; Janecke, A.R.
Chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1) deficiency results in a mild skeletal dysplasia and joint laxity
Hum. Mutat.
38
34-38
2017
Homo sapiens (Q8TDX6), Homo sapiens
brenda
Ji, X.Y.; Chen, J.H.; Zheng, G.H.; Huang, M.H.; Zhang, L.; Yi, H.; Jin, J.; Jiang, J.D.; Peng, Z.G.; Li, Z.R.
Design and synthesis of cajanine analogues against hepatitis C virus through down-regulating host chondroitin sulfate N-acetylgalactosaminyltransferase 1
J. Med. Chem.
59
10268-10284
2016
Homo sapiens (Q8TDX6)
brenda
Yoshioka, N.; Miyata, S.; Tamada, A.; Watanabe, Y.; Kawasaki, A.; Kitagawa, H.; Takao, K.; Miyakawa, T.; Takeuchi, K.; Igarashi, M.
Abnormalities in perineuronal nets and behavior in mice lacking CSGalNAcT1, a key enzyme in chondroitin sulfate synthesis
Mol. Brain
10
47
2017
Mus musculus (Q8BJQ9)
brenda
Clausen, T.M.; Pereira, M.A.; Al Nakouzi, N.; Oo, H.Z.; Agerbaek, M.O.; Lee, S.; Oerum-Madsen, M.S.; Kristensen, A.R.; El-Naggar, A.; Grandgenett, P.M.; Grem, J.L.; Hollingsworth, M.A.; Holst, P.J.; Theander, T.; Sorensen, P.H.; Daugaard, M.; Salanti, A.
Oncofetal chondroitin sulfate glycosaminoglycans are key players in integrin signaling and tumor cell motility
Mol. Cancer Res.
14
1288-1299
2016
Homo sapiens (Q8TDX6), Homo sapiens, Mus musculus (Q8BJQ9), Mus musculus, Mus musculus C57BL/6 (Q8BJQ9)
brenda
Igarashi, M.; Takeuchi, K.; Sugiyama, S.
Roles of CSGalNAcT1, a key enzyme in regulation of CS synthesis, in neuronal regeneration and plasticity
Neurochem. Int.
119
77-83
2018
Homo sapiens (Q8TDX6), Homo sapiens (Q8N6G5), Mus musculus (Q8BJQ9), Mus musculus (Q8C1F4)
brenda
Shimbo, M.; Suzuki, R.; Fuseya, S.; Sato, T.; Kiyohara, K.; Hagiwara, K.; Okada, R.; Wakui, H.; Tsunakawa, Y.; Watanabe, H.; Kimata, K.; Narimatsu, H.; Kudo, T.; Takahashi, S.
Postnatal lethality and chondrodysplasia in mice lacking both chondroitin sulfate N-acetylgalactosaminyltransferase-1 and -2
PLoS ONE
12
e0190333
2017
Mus musculus (Q8BJQ9), Mus musculus (Q8C1F4), Mus musculus C57BL/6 (Q8BJQ9), Mus musculus C57BL/6 (Q8C1F4)
brenda
Sakai, D.; Nakai, T.; Hiraishi, S.; Nakamura, Y.; Ando, K.; Naiki, M.; Watanabe, M.
Upregulation of glycosaminoglycan synthesis by neurotropin in nucleus pulposus cells via stimulation of chondroitin sulfate N-acetylgalactosaminyltransferase 1 a new approach to attenuation of intervertebral disc degeneration
PLoS ONE
13
e0202640
2018
Homo sapiens (Q8TDX6), Homo sapiens
brenda
Adhikara, I.M.; Yagi, K.; Mayasari, D.S.; Suzuki, Y.; Ikeda, K.; Ryanto, G.R.T.; Sasaki, N.; Rikitake, Y.; Nadanaka, S.; Kitagawa, H.; Miyata, O.; Igarashi, M.; Hirata, K.-I.; Emoto, N.
Chondroitin sulfate N-acetylgalactosaminyltransferase-2 impacts foam cell formation and atherosclerosis by altering macrophage glycosaminoglycan chain
Arterioscler. Thromb. Vasc. Biol.
41
1076-1091
2021
Mus musculus (Q8C1F4)
brenda
Inada, R.; Miyamoto, K.; Tanaka, N.; Moriguchi, K.; Kadomatsu, K.; Takeuchi, K.; Igarashi, M.; Kusunoki, S.
Chondroitin sulfate N-acetylgalactosyltransferase-1 knockout shows milder phenotype in experimental autoimmune encephalomyelitis than in wild type
Glycobiology
31
260-265
2021
Mus musculus (Q8BJQ9)
brenda
EXTERNAL LINKS (specific for EC-Number 2.4.1.174)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
