Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 UDP-N-acetyl-alpha-D-glucosamine + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-alpha-(1->6)-[D-Man-alpha-(1->3)]-D-Man-beta-(1->4)-D-GlcNAc
2 UDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-[D-GlcNAc-beta-(1->4)]-D-Man-alpha-(1->6)-[D-Man-alpha-(1->3)]-D-Man-beta-(1->4)-D-GlcNAc + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-alpha-(1->6)-[D-Man-alpha-(1->3)]-[D-GlcNAc-beta-(1->4)]-D-Man-beta-(1->4)-D-GlcNAc
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-(alpha-(1->2)-D-Man-alpha-(1->6)]-D-Man-alpha-(1->6)-[D-Man-(alpha-(1->2)-D-Man-(alpha-(1->2)-D-Man-alpha-(1->3)]-D-Man-beta-(1->4)-D-GlcNAc
UDP D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-(alpha-(1->2)-D-Man-alpha-(1->6)]-[D-GlcNAc-beta-(1->4)]-D-Man-alpha-(1->6)-[D-Man-(alpha-(1->2)-D-Man-(alpha-(1->2)-D-Man-alpha-(1->3)]-D-Man-beta-(1->4)-D-GlcNAc
-
-
-
?
UDP-N-acetyl-D-glucosamine + (mannose)9-N-acetyl-D-glucosamine
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + alpha-D-glucuronosyl-(1-4)-N-acetylglucoside
UDP + alpha-N-acetyl-D-glucosaminyl-alpha-D-glucuronosyl-(1-4)-N-acetylglucoside
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1,4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1,4)-beta-D-glucuronosyl-(1,4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP-N-acetyl-D-glucosamine + N-acetylheparosan oligosaccharide
?
with terminal nonreducing glucuronic acid
-
-
?
UDP-N-acetyl-D-glucosamine + [D-glucuronic acid-N-acetyl-glucosamine]14 -D-glucuronic acid-2,5-anhydro-D-mannose
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [D-glucuronic acid-N-acetyl-glucosamine]4 -D-glucuronic acid-2,5-anhydro-D-mannose
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseamin-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-[D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseaminyl-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
additional information
?
-
UDP-N-acetyl-D-glucosamine + alpha-D-glucuronosyl-(1-4)-N-acetylglucoside
UDP + alpha-N-acetyl-D-glucosaminyl-alpha-D-glucuronosyl-(1-4)-N-acetylglucoside
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + alpha-D-glucuronosyl-(1-4)-N-acetylglucoside
UDP + alpha-N-acetyl-D-glucosaminyl-alpha-D-glucuronosyl-(1-4)-N-acetylglucoside
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + [D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseamin-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-[D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseaminyl-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
-
octasaccharide but not nonasaccharide serves as acceptor
-
?
UDP-N-acetyl-D-glucosamine + [D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseamin-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-[D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseaminyl-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
-
substrate is produced by E. coli K5, acceptor ability increases with increasing chain length
-
-
?
UDP-N-acetyl-D-glucosamine + [D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseamin-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-[D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseaminyl-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
-
heptasaccharide and nonasaccharide serve as acceptors
-
-
?
UDP-N-acetyl-D-glucosamine + [D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseamin-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-[D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseaminyl-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
-
different activities observed for acetylated and sulfated acceptors
-
-
?
UDP-N-acetyl-D-glucosamine + [D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseamin-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-[D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseaminyl-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
-
heptasaccharide and nonasaccharide serve as acceptors
-
-
?
UDP-N-acetyl-D-glucosamine + [D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseamin-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-[D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseaminyl-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
-
different activities observed for acetylated and sulfated acceptors
-
-
?
UDP-N-acetyl-D-glucosamine + [D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseamin-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-[D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseaminyl-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
-
heptasaccharide and nonasaccharide serve as acceptors
-
-
?
UDP-N-acetyl-D-glucosamine + [D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseamin-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-[D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseaminyl-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
-
different activities observed for acetylated and sulfated acceptors
-
-
?
UDP-N-acetyl-D-glucosamine + [D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseamin-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-[D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseaminyl-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
-
different activities observed for acetylated and sulfated acceptors
-
-
?
UDP-N-acetyl-D-glucosamine + [D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseamin-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-[D-glucuronosyl-beta-(1->4)-N-acetyl-D-glucoseaminyl-alpha-(1->4)]n-D-glucuronosyl-2,5-anhydro-D-mannose
-
substrate is produced by E. coli K5, acceptor ability increases with increasing chain length
-
-
?
additional information
?
-
-
EXT1 and EXT2 proteins also acts as beta(1,4)-glucuronyltransferase (EC 2.4.1.225)
-
-
?
additional information
?
-
-
EXT1 and EXT2 proteins also acts as beta(1,4)-glucuronyltransferase (EC 2.4.1.225)
-
-
?
additional information
?
-
-
EXT1 and EXT2 proteins also acts as beta(1,4)-glucuronyltransferase (EC 2.4.1.225)
-
-
?
additional information
?
-
EXT1 and EXT2 proteins also acts as beta(1,4)-glucuronyltransferase (EC 2.4.1.225)
-
-
?
additional information
?
-
-
formation of homo- and heterooligomeric complexes of EXT1 and EXT2, heterooligomeric complexes have substantially higher glycosyltransferase activity than EXT1 or EXT2 has alone
-
-
?
additional information
?
-
-
different acceptors tested for activity with UDP-N-acetyl-D-glucosamine
-
-
?
additional information
?
-
-
EXT1 and EXT2 proteins also acts as beta(1,4)-glucuronyltransferase (EC 2.4.1.225)
-
-
?
additional information
?
-
-
different acceptors tested for activity with UDP-N-acetyl-D-glucosamine
-
-
?
additional information
?
-
-
formation of homo- and heterooligomeric complex of EXT1 and EXT2, heterooligomeric complexes have substantially higher glycosyltransferase activity than EXT1 or EXT2 has alone
-
-
?
additional information
?
-
-
the EXT1 and EXT2 hetero-oligomeric complex has glycosyltransferase activity that is essential for the synthesis and expression of heparan sulfate glycosaminoglycans
-
-
?
additional information
?
-
-
EXT1 and EXT2 proteins also acts as beta(1,4)-glucuronyltransferase (EC 2.4.1.225)
-
-
?
additional information
?
-
-
EXT1 and EXT2 proteins also acts as beta(1,4)-glucuronyltransferase (EC 2.4.1.225)
-
-
?
additional information
?
-
-
EXT1 and EXT2 proteins also acts as beta(1,4)-glucuronyltransferase (EC 2.4.1.225)
-
-
?
additional information
?
-
-
the Ext1/Ext2 complex possesses higher glycosyltransferase activity than Ext1 or Ext2 alone
-
-
?
additional information
?
-
-
the Ext1/Ext2 complex possesses higher glycosyltransferase activity than Ext1 or Ext2 alone
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
additional information
?
-
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan
-
elongation of growing chains of heparin and heparan sulfate, tumor suppressor
-
-
?
additional information
?
-
-
the Ext1/Ext2 complex possesses higher glycosyltransferase activity than Ext1 or Ext2 alone
-
-
?
additional information
?
-
-
the Ext1/Ext2 complex possesses higher glycosyltransferase activity than Ext1 or Ext2 alone
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Carcinoma
Exostosin1 as a novel prognostic and predictive biomarker for squamous cell lung carcinoma: A study based on bioinformatics analysis.
Diabetes Mellitus
Lack of replication of common EXT2 gene variants with susceptibility to type 2 diabetes in Lebanese Arabs.
Diabetes Mellitus, Type 2
Lack of replication of common EXT2 gene variants with susceptibility to type 2 diabetes in Lebanese Arabs.
Exostoses
Heparan sulfate deficiency leads to hypertrophic chondrocytes by increasing bone morphogenetic protein signaling.
Exostoses
Old gene, new phenotype: mutations in heparan sulfate synthesis enzyme, EXT2 leads to seizure and developmental disorder, no exostoses.
Exostoses
Structural analysis of glycosaminoglycans in animals bearing mutations in sugarless, sulfateless, and tout-velu. Drosophila homologues of vertebrate genes encoding glycosaminoglycan biosynthetic enzymes.
Exostoses, Multiple Hereditary
Case Report of the positive exostosin-1 without B-cell lymphoma-2 gene expression of giant cell tumor lesion in hereditary multiple exostosis.
Exostoses, Multiple Hereditary
Correlation between mutated genes and forearm deformity in patients with multiple osteochondroma.
Exostoses, Multiple Hereditary
Deletion of exon 8 from the EXT1 gene causes multiple osteochondromas (MO) in a family with three affected members.
Exostoses, Multiple Hereditary
Etiological point mutations in the hereditary multiple exostoses gene EXT1: a functional analysis of heparan sulfate polymerase activity.
Exostoses, Multiple Hereditary
Familial nephropathy and multiple exostoses with exostosin-1 (EXT1) gene mutation.
Exostoses, Multiple Hereditary
Heparan sulfate deficiency leads to hypertrophic chondrocytes by increasing bone morphogenetic protein signaling.
Exostoses, Multiple Hereditary
Identification and functional characterization of the human EXT1 promoter region.
Exostoses, Multiple Hereditary
Intraosseous atypical chondroid tumor or chondrosarcoma grade 1 in patients with multiple osteochondromas.
Exostoses, Multiple Hereditary
Large-scale mutational analysis in the EXT1 and EXT2 genes for Japanese patients with multiple osteochondromas.
Exostoses, Multiple Hereditary
Multiple osteochondromas: clinicopathological and genetic spectrum and suggestions for clinical management.
Exostoses, Multiple Hereditary
Novel and recurrent mutations in the EXT1 and EXT2 genes in Chinese kindreds with multiple osteochondromas.
Exostoses, Multiple Hereditary
Novel exostosin-2 mutation identified in a Chinese family with hereditary multiple osteochondroma.
Exostoses, Multiple Hereditary
Somatic loss of an EXT2 gene mutation during malignant progression in a patient with hereditary multiple osteochondromas.
Exostoses, Multiple Hereditary
Targeted Next-Generation Sequencing Newly Identifies Mutations in Exostosin-1 and Exostosin-2 Genes of Patients with Multiple Osteochondromas.
Giant Cell Tumors
Case Report of the positive exostosin-1 without B-cell lymphoma-2 gene expression of giant cell tumor lesion in hereditary multiple exostosis.
Infections
Enterovirus 71 uses cell surface heparan sulfate glycosaminoglycan as an attachment receptor.
Intellectual Disability
Novel exostosin-2 missense variants in a family with autosomal recessive exostosin-2-related syndrome: further evidences on the phenotype.
Neoplasms
Case Report of the positive exostosin-1 without B-cell lymphoma-2 gene expression of giant cell tumor lesion in hereditary multiple exostosis.
Neoplasms
Deletion of exon 8 from the EXT1 gene causes multiple osteochondromas (MO) in a family with three affected members.
Neoplasms
Epigenetic loss of the familial tumor-suppressor gene exostosin-1 (EXT1) disrupts heparan sulfate synthesis in cancer cells.
Neoplasms
Increased EXT1 gene copy number correlates with increased mRNA level predicts short disease-free survival in hepatocellular carcinoma without vascular invasion.
Neoplasms
Multiple osteochondromas: clinicopathological and genetic spectrum and suggestions for clinical management.
Neoplasms
Structural analysis of glycosaminoglycans in Drosophila and Caenorhabditis elegans and demonstration that tout-velu, a Drosophila gene related to EXT tumor suppressors, affects heparan sulfate in vivo.
Neoplasms
Tout-velu is a Drosophila homologue of the putative tumour suppressor EXT-1 and is needed for Hh diffusion.
Seizures
Novel exostosin-2 missense variants in a family with autosomal recessive exostosin-2-related syndrome: further evidences on the phenotype.
Seizures
Old gene, new phenotype: mutations in heparan sulfate synthesis enzyme, EXT2 leads to seizure and developmental disorder, no exostoses.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
-
EXT1 influences fibroblast matrix interactions. Essential role of EXT1 in providing specific binding sites for growth factors and extracellular matrix proteins. Phosphorylation of ERK1/2 in response to FGF2 stimulation is markedly decreased in the Ext1 mutant fibroblasts, whereas neither PDGF-BB nor FGF10 signaling is significantly affected. Ext1 mutants display reduced ability to attach to collagen I and to contract collagen lattices. Reintroduction of Ext1 in Ext1 mutant fibroblasts rescues heparan sulfate chain length, FGF2 signaling, and the ability of the fibroblasts to contract collagen
malfunction
-
a reduction in either Ext1 or Ext2 can cause a reduction in heparan sulfate biosynthesis, overview. Suppression of Ext1 by siRNA in FBJ-S1 cells results in the decreased expression of heparan sulfate and enhanced motility
malfunction
-
conditional Ext1 mutant mice display severe limb skeletal defects, including shortened and malformed limb bones, oligodactyly, and fusion of joints. the segregation of the pSmad1/5/8-expressing chondrocytes and fibronectin-expressing perichondrium-like cells surrounding chondrocyte nodules is disrupted in mutant micromass cultures, Ext2-mutant phenotypes, detailed overview
malfunction
-
Fgf targeted gene expression is reduced in ext2 mutants and the remaining expression is readily inhibited by SU5402, an FGF receptor inhibitor. In the ext2 mutants, Fgf signaling is affected during nervous system development, mechanism, overview, and reduction of Fgf ligands in the mutants affects tail development. Wnt signaling is also affected in the ext2 mutants, while Hh dependent signaling is apparently unaffected in the ext2 mutants, Hh targeted gene expression is not reduced, the Hh inhibitor cyclopamine is not more affective in the mutants and Hh-dependent cell differentiation in the retina and in the myotome are normal in ext2 mutants, ext2 mutant phenotypes, overview
malfunction
deletion of Ext1 in the mesoderm induces a cardiac phenotype similar to that of a mutant with conditional deletion of UDP-glucose dehydrogenase, a key enzyme responsible for synthesis of all glycosaminoglycans. The outflow tract defect in conditional Ext1 knockout (Ext1f/f:Mesp1Cre) mice is attributable to the reduced contribution of second heart field and neural crest cells. Ext1 deletion leads to downregulation of FGF signaling in the pharyngeal mesoderm. Exogenous FGF8 ameliorates the defects in the outflow tract and pharyngeal explants. Phenotype, detailed overview
malfunction
ectopic cartilage forms in Ext1-deficient mouse embryo long bones, phenotype overview. perichondrium phenotype and border function regulation is deregulated in hereditary multiple exostoses. Ext1 deficiency stimulates cartilage formation
malfunction
effect of heterozygous mutations in heparan sulfate elongation genes EXT1 and EXT2 on endothelial function in vitro as well as in vivo, phenotype, overview
malfunction
effect of heterozygous mutations in heparan sulfate elongation genes EXT1 and EXT2 on endothelial function in vitro as well as in vivo. Silencing of microvascular endothelial cell EXT1 and EXT2 under flow led to significant upregulation of endothelial nitric oxide synthesis and phospho-endothelial nitric oxide synthesis protein expression. Brachial artery flow-mediated dilation is significantly increased in hereditary multiple exostoses (HME) patients. In humans, heterozygous loss of function mutation in EXT1 and EXT2 are known to be involved in the development of HME syndrome, a disorder associated with bony tumor formation. In these humans, the loss-of-function mutations lead to alterations in the structure of tissue and plasma heparan sulfate composition, phenotype, overview
malfunction
mutations in the tumor suppressor genes EXT1 and EXT2 disturb heparan sulfate proteoglycan biosynthesis and cause multiple osteochondroma. A reduction in Rti shifts the steady-state distribution of EXTs to the trans-Golgi. These accumulated EXTs tend to be degraded and their re-entrance towards the route for polymerizing GAG chains is disengaged. Conversely, EXTs are mislocalized towards the transitional endoplasmic reticulum/cis-Golgi when Rti is overexpressed. Both loss of function and overexpression of rti result in incomplete heparan sulfate proteoglycans and perturb Hedgehog signaling
malfunction
phenotype of four patients showing clinical seizures-scoliosis-macrocephaly syndrome with seizures and macrocephaly due to decreased EXT2 expression and mutations M87R and R95C. SSM syndrome is characterised by seizures, intellectual disability, hypotonia, scoliosis, macrocephaly, hypertelorism and renal dysfunction. Phenotype, overview
malfunction
Ext1 knock-down reduces heparan sulfate, and increases chondrogenic markers and proteoglycan accumulation. Ext1 knock-down reduces active Wnt/beta-catenin signaling
malfunction
screening and identifying the gene mutation of EXT1 associated with multiple exostosis and the expression in tumor tissues
malfunction
-
a reduction in either Ext1 or Ext2 can cause a reduction in heparan sulfate biosynthesis, overview. Suppression of Ext1 by siRNA in FBJ-S1 cells results in the decreased expression of heparan sulfate and enhanced motility
-
malfunction
-
conditional Ext1 mutant mice display severe limb skeletal defects, including shortened and malformed limb bones, oligodactyly, and fusion of joints. the segregation of the pSmad1/5/8-expressing chondrocytes and fibronectin-expressing perichondrium-like cells surrounding chondrocyte nodules is disrupted in mutant micromass cultures, Ext2-mutant phenotypes, detailed overview
-
metabolism
Exostosin glycosyltransferases exclusively catalyze heparan sulfate polymerization. Heparan sulfate/heparin, chondroitin sulfate, dermatan sulfate, and keratan sulfate form glycosaminoglycans, long linear polysaccharide chains consisting of repeat disaccharide units. Glycosaminoglycans are the major components of the extracellular matrix and play critical roles in regulating transport and signaling of numerous growth factors during embryonic development
metabolism
the enzymes is involved in heparan sulfate biosynthesis. EXT1, NDST1, and NDST2 differentially regulate heparan sulfate biosynthesis in human tooth germ
physiological function
-
in patients with hereditary multiple exostoses, functional loss of EXT1 results in exostoses (osteochondromas), but inactivation of both copies of the gene (germline mutation plus loss of the remaining wild-type allele) is not required for development of the bone lesions. No reported association between EXT1 abnormalities and renal disease. Deficiency of heparan sulfate and perlecan, together with accumulation of collagens, in the matrix of EXT1-associated osteochondromas
physiological function
-
Ext1 and Ext2 are tumor suppressors. In the biosynthesis of heparan sulfate, after the attachment of a GlcNAc residue to GlcA-Gal-Gal-Xyl, Ext1 and Ext2 catalyze the subsequent elongation of glycosaminoglycans by alternately adding GlcA and GlcNAc to the end of the growing chain. Involvement of Ext1 and heparanase in migration of FBJ osteosarcoma cells, overview
physiological function
-
Ext1 and Ext2 together form a copolymerase which is responsible for the polymerization process where repeating units of N-acetylglucosamine and glucuronic acid are incorporated in the growing linear polysaccharide chain, see also EC 2.4.1.225. Gene ext2 is involved in Fgf and Wnt signaling but not in Hh signaling, ext2 is a general enhancer of Fgf target gene expression, ext2 interacts genetically with Fgf signaling during tail development, specificity for gene ext2 in signaling pathways during embryonic development, overview
physiological function
-
Ext1 encodes an essential glycosyltransferase for heparan sulfate synthesis, heparan sulfate is essential for patterning of limb skeletal elements
physiological function
exostosin (EXT) genes encode glycosyltransferases required for glycosaminoglycan chain polymerization in the biosynthesis of heparan sulfate proteoglycans. Synthesis of heparan sulfate proteoglycans requires sequential enzymatic modifications of glycoproteins in the Golgi. Drosophila Golgi phosphoprotein 3, GOLPH3 or rotini, Rti, regulates the biosynthesis of heparan sulfate proteoglycans by modulating the retrograde trafficking of exostosins. Rti regulates the stability of EXTs
physiological function
exostosin (EXT) genes encode glycosyltransferases required for glycosaminoglycan chain polymerization in the biosynthesis of heparan sulfate proteoglycans. Synthesis of heparan sulfate proteoglycans requires sequential enzymatic modifications of glycoproteins in the Golgi. Drosophila Golgi phosphoprotein 3, GOLPH3 or rotini, Rti, regulates the biosynthesis of heparan sulfate proteoglycans by modulating the retrograde trafficking of exostosins. Rti regulates the stability of EXTs. Proper function of EXTs depends not only on their enzymatic activities but also on their sub-compartmental distributions
physiological function
Ext1 is a glycosyltransferase responsible for heparan sulfate synthesis. Function of Ext1 in heart development, overview. Ext1 expression in second heart field and neural crest cells is required for outflow tract remodeling. Ext1 is crucial for outflow tract formation in distinct progenitor cells, and heparan sulfate modulates FGF signaling during early heart development. Proper expression of Ext1 is required for cardiogenesis, heparan sulfate is required for heart development
physiological function
heparan sulfate elongation genes EXT1 and EXT2 are involved in heparan sulfate elongation and in maintaining endothelial homeostasis, presumably via increased nitric oxide bioavailability
physiological function
heparan sulfate elongation genes EXT1 and EXT2 are involved in heparan sulfate elongation and in maintaining endothelial homeostasis, presumably via increased nitric oxide bioavailability
physiological function
perichondrium phenotype and border function are deranged by Ext1 and heparan sulfate in developing long bones, and in ectopic cartilage formation
physiological function
key enzyme contributing to the generation of heparan sulfate chains. EXT1, with tumour suppressor properties, is involved in the initiation and polymerisation of the growing heparan sulfate chain. The study may suggest that no association exists between EXT1 and multiple sclerosis
physiological function
key enzymes contributing to the generation of heparan sulfate chains. EXT1, with documented tumour suppressor properties, is involved in the initiation and polymerisation of the growing heparan sulfate chain
physiological function
the enzyme is involved in heparan sulfate biosynthesis
physiological function
the enzyme is required for heparan sulfate chain elongation in heparan sulfate-proteoglycan biosynthesis. EXT1 affects chondrogenic differentiation of precursor cells, in part via changes in the activity of Wnt/beta-catenin signaling. Wnt/beta-catenin signaling controls Ext1 expression, suggesting a regulatory loop between EXT1 and Wnt/beta-catenin signaling during chondrogenesis
physiological function
-
Ext1 and Ext2 are tumor suppressors. In the biosynthesis of heparan sulfate, after the attachment of a GlcNAc residue to GlcA-Gal-Gal-Xyl, Ext1 and Ext2 catalyze the subsequent elongation of glycosaminoglycans by alternately adding GlcA and GlcNAc to the end of the growing chain. Involvement of Ext1 and heparanase in migration of FBJ osteosarcoma cells, overview
-
physiological function
-
Ext1 encodes an essential glycosyltransferase for heparan sulfate synthesis, heparan sulfate is essential for patterning of limb skeletal elements
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Sharkey, D.J.; Kornfeld, R.
Identification of an N-acetylglucosaminyltransferase in Dictyostelium discoideum that transfers an intersecting N-acetylglucosamine residue to high mannose oligosaccharides
J. Biol. Chem.
264
10411-10419
1989
Dictyostelium discoideum
brenda
Kitagawa, H.; Egusa, N.; Tamura, J.I.; Kusche-Gullberg, M.; Lindahl, U.; Sugahara, K.
rib-2, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes encodes a novel alpha-1,4-N-acetylglucosaminyltransferase involved in the biosynthetic initiation and elongation of heparan sulfate
J. Biol. Chem.
276
4834-4838
2001
Caenorhabditis elegans, Homo sapiens
brenda
Senay, C.; Lind, T.; Muguruma, K.; Tone, Y.; Kitagawa, H.; Sugahara, K.; Lidholt, K.; Lindahl, U.; Kusche-Gullberg, M.
The EXT1/EXT2 tumor suppressors: catalytic activities and role in heparan sulfate biosynthesis
EMBO Rep.
1
282-286
2000
Bos taurus, Mus musculus, no activity in yeast
brenda
Lind, T.; Tufaro, F.; McCormick, C.; Lindahl, U.; Lidholt, K.
The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate
J. Biol. Chem.
273
26265-26268
1998
Mus musculus, Bos taurus (O77783)
brenda
Lidholt, K.; Lindahl, U.
Biosynthesis of heparin. The D-glucuronosyl- and N-acetyl-D-glucosaminyltransferase reactions and their relation to polymer modification
Biochem. J.
287
21-29
1992
Bos taurus, Mus musculus
-
brenda
Lind, T.; Lindahl, U.; Lidholt, K.
Biosynthesis of heparin/heparan sulfate. Identification of a 70-kDa protein catalyzing both the D-glucuronosyl- and the N-acetyl-D-glucosaminyltransferase reactions
J. Biol. Chem.
268
20705-20708
1993
Bos taurus
brenda
Lidholt, K.; Fjelstad, M.; Jann, K.; Lindahl, U.
Biosynthesis of heparin. XXV. Substrate specificities of glucosyltransferases involved in formation of heparin precursor and E. coli K5 capsular polysaccharides
Carbohydr. Res.
255
87-101
1994
Escherichia coli, Mus musculus, Escherichia coli O18:K5
brenda
Lind, T.
Enzymes involved in heparan sulfate chain elongation
Trends Glycosci. Glycotechnol.
11
221-225
1999
Bos taurus, Cricetinae
-
brenda
Wei, G.; Bai, X.; Gabb, M.M.G.; Bame, K.J.; Koshy, T.I.; Spear, P.G.; Esko, J.D.
Location of the glucuronosyltransferase domain in the heparan sulfate copolymerase EXT1 by analysis of Chinese hamster ovary cell mutants
J. Biol. Chem.
275
27733-27740
2000
Cricetinae, Homo sapiens, Mus musculus
brenda
Kim, B.T.; Kitagawa, H.; Tamura, J.I.; Saito, T.; Kusche-Gullberg, M.; Lindahl, U.; Sugahara, K.
Human tumor suppressor EXT gene family members EXTL1 and EXTL3 encode alpha-1,4-N-acetylglucosaminyltransferases that likely are involved in heparan sulfate/heparin biosynthesis
Proc. Natl. Acad. Sci. USA
98
7176-7181
2001
Homo sapiens
brenda
Kim, B.T.; Kitagawa, H.; Tamura, J.I.; Kusche-Gullberg, M.; Lindahl, U.; Sugahara, K.
Demonstration of a novel gene DEXT3 of Drosophila melanogaster as the essential N-acetylglucosamine transferase in the heparan sulfate biosynthesis: Chain initiation and elongation
J. Biol. Chem.
277
13659-13665
2002
Drosophila melanogaster (Q9XZ08)
brenda
McCormic, C.; Leduc, Y.; Martindale, D.; Mattison, K.; Esford, L.E.; Dyer, A.P.; Tufaro, F.
The putative tumor suppressor EXT 1 alters the expression of cell surface heparan sulfate
Nat. Genet.
19
158-161
1998
Cricetinae, Mus musculus
brenda
Han, C.; Belenkaya, T.Y.; Khodoun, M.; Tauchi, M.; Lin, X.; Lin, X.
Distinct and collaborative roles of Drosophila EXT family proteins in morphopgen signalling and gradient formation
Development
131
1563-1575
2005
Drosophila melanogaster
brenda
Bornemann, D.J.; Duncan, J.E.; Staatz, W.; Selleck, S.; Warrior, R.
Abrogation of heparan sulfate synthesis in Drosophila disrupts the Wingless, Hedgehog and Decapentaplegic signaling pathways
Development
131
1927-198
2004
Drosophila melanogaster
brenda
Wuyts, W.; van Hul, W.
Molecular basis of multiple exostoses: mutations in the EXT1 and EXT2 genes
Hum. Mutat.
15
220-227
2000
Homo sapiens
brenda
Busse, M.; Kusche-Gullberg, M.
In vitro polymerization of heparan sulfate backbone by the EXT proteins
J. Biol. Chem.
278
41333-41337
2003
Homo sapiens
brenda
McCormick, C.; Duncan, G.; Goutsos, K.T.; Tufaro, F.
The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heapran sulfate
Proc. Natl. Acad. Sci. USA
97
668-673
2000
Bos taurus, Homo sapiens
brenda
Chen, M.; Bridges, A.; Liu, J.
Determination of the substrate specificities of N-acetyl-D-glucosaminyltransferase
Biochemistry
45
12358-12365
2006
Escherichia coli
brenda
Hecht, J.T.; Hayes, E.; Haynes, R.; Cole, W.G.; Long, R.J.; Farach-Carson, M.C.; Carson, D.D.
Differentiation-induced loss of heparan sulfate in human exostosis derived chondrocytes
Differentiation
73
212-221
2005
Homo sapiens (Q16394), Homo sapiens (Q93063)
brenda
Murakami, K.; Namikawa, K.; Shimizu, T.; Shirasawa, T.; Yoshida, S.; Kiyama, H.
Nerve injury induces the expression of EXT2, a glycosyltransferase required for heparan sulfate synthesis
Neuroscience
141
1961-1969
2006
Mus musculus
brenda
Roberts, I.S.; Gleadle, J.M.
Familial nephropathy and multiple exostoses with exostosin-1 (EXT1) gene mutation
J. Am. Soc. Nephrol.
19
450-453
2008
Homo sapiens
brenda
Osterholm, C.; Barczyk, M.M.; Busse, M.; Gronning, M.; Reed, R.K.; Kusche-Gullberg, M.
Mutation in the heparan sulfate biosynthesis enzyme EXT1 influences growth factor signaling and fibroblast interactions with the extracellular matrix
J. Biol. Chem.
284
34935-34943
2009
Mus musculus
brenda
Fischer, S.; Filipek-Gorniok, B.; Ledin, J.
Zebrafish Ext2 is necessary for Fgf and Wnt signaling, but not for Hh signaling
BMC Dev. Biol.
11
53
2011
Danio rerio
brenda
Matsumoto, Y.; Matsumoto, K.; Irie, F.; Fukushi, J.; Stallcup, W.B.; Yamaguchi, Y.
Conditional ablation of the heparan sulfate-synthesizing enzyme Ext1 leads to dysregulation of bone morphogenic protein signaling and severe skeletal defects
J. Biol. Chem.
285
19227-19234
2010
Mus musculus, Mus musculus C57BL/6
brenda
Wang, Y.; Yang, X.; Yamagata, S.; Yamagata, T.; Sato, T.
Involvement of Ext1 and heparanase in migration of mouse FBJ osteosarcoma cells
Mol. Cell. Biochem.
373
63-72
2013
Mus musculus, Mus musculus BALB/c
brenda
Huegel, J.; Mundy, C.; Sgariglia, F.; Nygren, P.; Billings, P.C.; Yamaguchi, Y.; Koyama, E.; Pacifici, M.
Perichondrium phenotype and border function are regulated by Ext1 and heparan sulfate in developing long bones: a mechanism likely deranged in hereditary multiple exostoses
Dev. Biol.
377
100-112
2013
Mus musculus (P97464)
brenda
Chang, W.L.; Chang, C.W.; Chang, Y.Y.; Sung, H.H.; Lin, M.D.; Chang, S.C.; Chen, C.H.; Huang, C.W.; Tung, K.S.; Chou, T.B.
The Drosophila GOLPH3 homolog regulates the biosynthesis of heparan sulfate proteoglycans by modulating the retrograde trafficking of exostosins
Development
140
2798-2807
2013
Drosophila melanogaster (Q9V730), Drosophila melanogaster (Q9Y169)
brenda
Mooij, H.L.; Cabrales, P.; Bernelot Moens, S.J.; Xu, D.; Udayappan, S.D.; Tsai, A.G.; van der Sande, M.A.; de Groot, E.; Intaglietta, M.; Kastelein, J.J.; Dallinga-Thie, G.M.; Esko, J.D.; Stroes, E.S.; Nieuwdorp, M.
Loss of function in heparan sulfate elongation genes EXT1 and EXT 2 results in improved nitric oxide bioavailability and endothelial function
J. Am. Heart Assoc.
3
e001274
2014
Mus musculus (P70428), Mus musculus (P97464), Homo sapiens (Q16394), Homo sapiens (Q93063)
brenda
Farhan, S.M.; Wang, J.; Robinson, J.F.; Prasad, A.N.; Rupar, C.A.; Siu, V.M.; Siu, V.M.; Hegele, R.A.
Old gene, new phenotype: mutations in heparan sulfate synthesis enzyme, EXT2 leads to seizure and developmental disorder, no exostoses
J. Med. Genet.
52
666-675
2015
Homo sapiens (Q93063), Homo sapiens
brenda
Zhang, R.; Cao, P.; Yang, Z.; Wang, Z.; Wu, J.L.; Chen, Y.; Pan, Y.
Heparan sulfate biosynthesis enzyme, Ext1, contributes to outflow tract development of mouse heart via modulation of FGF signaling
PLoS ONE
10
e0136518
2015
Mus musculus (P97464)
brenda
Wu, Z.; Wang, Y.; Wang, J.; Chen, Y.; Guo, Y.
The role of EXT1 gene mutation and its high expression of calcitonin gene-related peptide in the development of multiple exostosis
Biochem. Biophys. Res. Commun.
505
959-965
2018
Homo sapiens (Q16394)
brenda
Sembajwe, L.; Katta, K.; Gronning, M.; Kusche-Gullberg, M.
The exostosin family of glycosyltransferases MRNA expression profiles and heparan sulphate structure in human breast carcinoma cell lines
Biosci. Rep.
38
1-12
2018
Homo sapiens (Q16394), Homo sapiens (Q93063)
brenda
Kero, D.; Bilandzija, T.; Arapovic, L.; Vukojevic, K.; Saraga-Babic, M.
Syndecans and enzymes involved in heparan sulfate biosynthesis and degradation are differentially expressed during human dontogenesis
Front. Physiol.
9
732
2018
Homo sapiens (Q16394)
brenda
Okolicsanyi, R.K.; Bluhm, J.; Miller, C.; Griffiths, L.R.; Haupt, L.M.
An investigation of genetic polymorphisms in heparan sulfate proteoglycan core proteins and key modification enzymes in an Australian Caucasian multiple sclerosis population
Hum. Genomics
14
18
2020
Homo sapiens (Q16394)
brenda
Ushakov, V.; Tsidulko, A.; De La Bourdonnaye, G.; Kazanskaya, G.; Volkov, A.; Kiselev, R.; Kobozev, V.; Kostromskaya, D.; Gaytan, A.; Krivoshapkin, A.; Aidagulova, S.; Grigorieva, E.
Heparan sulfate biosynthetic system is inhibited in human glioma due to EXT1/2 and HS6ST1/2 down-regulation
Int. J. Mol. Sci.
18
2301
2017
Homo sapiens (Q16394), Homo sapiens (Q93063)
brenda
Wang, X.; Cornelis, F.M.F.; Lories, R.J.; Monteagudo, S.
Exostosin-1 enhances canonical Wnt signaling activity during chondrogenic differentiation
Osteoarthritis Cartilage
27
1702-1710
2019
Homo sapiens (Q16394), Homo sapiens
brenda