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Information on EC 2.4.1.150 - N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase and Organism(s) Homo sapiens
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2.4.1.150 N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferaseIUBMB Comments
The enzyme acts on poly-N-acetyllactosamine [glycan chains of beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine units connected by beta(1,3) linkages] attached to proteins or lipids. It transfers a GlcNAc residue by beta(1,6)-linkage to galactosyl residues close to non-reducing terminals, introducing a branching pattern known as I branching.
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Word Map
- 2.4.1.150
- cataract
- poly-n-acetyllactosamine
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cryaa
- n-acetyllactosamine
-
polylactosamines
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glycan-binding
- diagnostics
- pharmacology
- medicine
- synthesis
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
gcnt2, i-branching enzyme, glucosaminyl (n-acetyl) transferase 2, i-branching beta-1,6-n-acetylglucosaminyltransferase, i-branching n-acetylglucosaminyltransferase, i n-acetylglucosaminyltransferase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-acetyllactosaminide beta1-->6-
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beta1-6GnT
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Galbeta1-->4GlcNAc-R beta1-->6 N-acetylglucosaminyltransferase
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GCNT2
gcnt3
I N-acetylglucosaminyltransferase
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IGnT
N-acetylglucosaminyltransferase
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N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase
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UDP-GlcNAc:Gal-R, beta-D-6-N-acetylglucosaminyltransferase
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UDP-N-acetyl-D-glucosamine:beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminide 6-beta-N-acetyl-D-glucosaminyltransferase
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uridine diphosphoacetylglucosamine-acetyllactosaminide beta1-->6-acetylglucosaminyltransferase
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additional information
IGnT
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additional information
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C2GnT forms the core 2 O-glycan branch, IGnT forms the I antigen, both are members of a beta-1,6-N-acetylglucosaminyltransferase gene family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminide 6-beta-N-acetylglucosaminyltransferase (configuration-inverting)
The enzyme acts on poly-N-acetyllactosamine [glycan chains of beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine units connected by beta(1,3) linkages] attached to proteins or lipids. It transfers a GlcNAc residue by beta(1,6)-linkage to galactosyl residues close to non-reducing terminals, introducing a branching pattern known as I branching.
CAS REGISTRY NUMBER
COMMENTARY
85638-40-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + asialo-alpha1-acid glycoprotein
UDP + N-acetylglucosaminylated asialo-alpha1-acid glycoprotein
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acts on beta-galactosyl-1,4-N-acetylglucosaminyl-termini on asialo-alpha1-acid glycoproteins
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?
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP-N-acetyl-D-glucosamine + Galalpha(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
?
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reaction rate is 38% of that with GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
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?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAc
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cIGnT
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?
UDP-N-acetyl-D-glucosamine + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + (GlcNAc)1-Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
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cIGnT
also as product: (GlcNAc)2-Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc, cIGnT6 generates in a partial reaction nona- and decasaccharide products, which represent mixtures of isomers carrying one or two GlcNAc-branches on the linear octasaccharide acceptor
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAc
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very poor acceptor, reaction rate is 2% of that with GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
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?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Gal
?
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poor acceptor, reaction rate is 6% of that with GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
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?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)Glc
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reaction rate is 41% of that with GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
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?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc
UDP + GlcNAcbeta(1-3)Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)GlcNAc
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GlcNAc residue at the reducing end side of the branching galactose plays a role in the reaction
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?
UDP-N-acetyl-D-glucosamine + lactose
UDP + GlcNAcbeta(1-6)Galbeta(1-4)Glc
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?
UDP-N-acetyl-D-glucosamine + N-acetyllactosamine
UDP + GlcNAcbeta(1-6)Galbeta(1-4)GlcNAc
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UDP-N-acetyl-D-glucosamine + oligo-N-acetyllactosaminoglycan
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involved in midchain branching of oligo-N-acetyllactosaminoglycans by transferring GlcNAc in beta1,6-linkage to internal galactose residues
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UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
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?
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
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acts on beta-galactosyl-1,4-N-acetylglucosaminyl-termini on asialo-alpha1-acid glycoproteins
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?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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forms branches in poly-N-acetyllactosamines
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?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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transfer of GlcNAc to beta1,4-linked Gal residue in a linear poly-N-acetyllactosamine with the approximate structure Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc(NAc)-R, forming Galbeta(1-4)GlcNAcbeta(1-3)(GlcNAcbeta(1-6))Galbeta(1-4)Glc(NAc)-R
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?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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cIGnT6 transfers one or multiple GlcNAc branches to midchain galactoses of long linear polylactosamines
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?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
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responsible for the conversion of linear to branched polylactosamines, cIGnT6 actions at central rather than peridistal galactose residues of linear polylactosamines in the biosynthesis of blood group I antigens
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?
additional information
?
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2 types of branching enzyme activities: cIGnT6 generates beta-1,6-N-acetylglucosaminyl branches at the central galactose residue, and dIGnT6 acts on peridistal galactose residues
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?
additional information
?
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2 types of branching enzyme activities: cIGnT6 generates beta-1,6-N-acetylglucosaminyl branches at the central galactose residue, and dIGnT6 acts on peridistal galactose residues
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?
additional information
?
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no substrate of cIGnT6: GlcNAcbeta(1-3)Galbeta(1-4)GlcNAc, Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)(Fucalpha(1-3))GlcNAc, no transfer of GlcNAc to substrates with alpha1-3-fucosyl residues and to midchain galactoses that belongs to Lewis x determinants
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?
additional information
?
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initiates formation of side chains, key enzyme in biosynthesis of I antigen of erythrocytes, N-acetyllactosamine is a more physiological acceptor than lactose
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?
additional information
?
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expression of I-antigen is entirely dependent on IGnT, expression of IGnT is developmentally regulated
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?
additional information
?
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C2GnT forms the core 2 O-glycan branch, which is critical for oligosaccharide-mediated cell-cell interaction, IGnT forms the I antigen, both are members of a beta-1,6-N-acetylglucosaminyltransferase gene family
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + oligo-N-acetyllactosaminoglycan
?
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involved in midchain branching of oligo-N-acetyllactosaminoglycans by transferring GlcNAc in beta1,6-linkage to internal galactose residues
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?
UDP-N-acetyl-D-glucosamine + poly-N-acetyllactosamine
?
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responsible for the conversion of linear to branched polylactosamines, cIGnT6 actions at central rather than peridistal galactose residues of linear polylactosamines in the biosynthesis of blood group I antigens
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?
additional information
?
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initiates formation of side chains, key enzyme in biosynthesis of I antigen of erythrocytes, N-acetyllactosamine is a more physiological acceptor than lactose
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?
additional information
?
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expression of I-antigen is entirely dependent on IGnT, expression of IGnT is developmentally regulated
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?
additional information
?
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C2GnT forms the core 2 O-glycan branch, which is critical for oligosaccharide-mediated cell-cell interaction, IGnT forms the I antigen, both are members of a beta-1,6-N-acetylglucosaminyltransferase gene family
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene contains three highly similar variable exons and two constant exons, each variable exon is preceded by a distinct promoter and is separately spliced to a set of two constant exons to generate functional Gcnt2 mRNA
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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IGnT is highly expressed in adult cerebellum and the frontal lobe of adult brain, also expression in fetal brain
GCNT2 is overexpressed in highly metastatic breast cancer cell lines. GCNT2 expression is also significantly correlated to the metastatic phenotype in breast tumor samples
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GCNT3 gene expression is downregulated in colorectal cancer (CRC) samples in comparison to non-pathological colon tissue
expression of GCNT2 is significantly higher in tumour tissues than in paratumour tissues, tissue microarray analysis
GCNT3 expression in Epstein-Barr virus (EBV)-associated gastric cancer cells and tissues is lower than in EBV-negative gastric cancer cells (EBVnGC) and tissues, and high expression is significantly associated with advanced tumor-lymph node metastasis. GCNT3 is closely related to the ERK signaling pathway and epithelial mesenchymal transition (EMT), regulating cell proliferation, migration, and invasion
GCNT3 is highly expressed in both NSCLC tissues and cell lines
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EOC, GCNT3 expression is analyzed in a cohort of 56 EOC patients followed by a meta-analysis of more than one thousand patients
over 95% of human pancreatic cancers are associated with Kras mutations
additional information
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tetracarcinoma cells, IGnT mainly acts as cIGnT, but can also act as dIGnT with 6-30% of the activity of cIGnT
additional information
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high expression of C2GnT in granulocyte-monocyte cell lineage
additional information
GCNT3 is highly expressed in both NSCLC tissues and cell lines, and higher expression is significantly associated with advanced tumor lymph node metastasis (TNM) stage, positive lymph node metastasis, and poor overall survival. GCNT3 expression is associated with lymph node metastasis and age. But the expression level of GCNT3 is not correlated with gender, tumor location, differentiation grade, etc. Expression of GCNT3 is lower in EBVaGC cells and tissues than that in EBVnGC cells and tissues
additional information
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integrated transcriptomic and proteomic analyses reveal that GCNT3 is linked to cellular cycle, mitosis and proliferation. The non-invasive HT-29 cell line, that is isolated from a primary tumor, shows GCNT3 expression (mRNA and protein). By contrast, cells belonging to metastatic and invasive SW family, e.g. SW620 and SW5FU, do not exhibit measurable GCNT3 expression
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
analysis of pleiotropic effect of mutations in GCNT2, especially frameshift mutation N388R, causing congenital cataract and a rare adult I blood group phenotype, detailed overview
malfunction
ectopic overexpression of GCNT2 enhances cell detachment, adhesion to endothelial cells, cell migration and invasion in vitro, and lung metastasis of breast cancer cells in vivo. Knockdown of GCNT2 expression decreases cell migration and invasion in vitro and lung metastasis in vivo. Diminution of the glycosyltransferase activity of I-branching beta-1,6-N-acetylglucosaminyl transferase 2 (GCNT2) abrogates its cell migration and invasion-promoting function and synergistic effect with TGF-beta to induce EMT, effect of GCNT2 expression knockdown on oncogenic properties, overview
malfunction
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GCNT3 overexpression reduces 5-fluorouracil resistance in colorectal cancer (CRC) cells. GCNT3 overexpression reduces proliferation, invasion and changes metabolic capacities of CRC cells. The enzyme's overexpression in epithelial ovarian cancer (EOC) patients is associated with better clinical outcome and response to initial therapy
malfunction
manipulation of I-branching N-acetylglucosaminyltransferase (GCNT2) expression in esophageal squamous cell carcinoma cells has no effect on cell proliferation. Overexpression of GCNT2 promotes the migration and invasion, and this effect is associated with increased expression of N-cadherin and vimentin and decreased expression of E-cadherin in KYSE30 and EC9706 cells. Knockdown of GCNT2 decreased the expression of N-cadherin and vimentin, increases the expression of E-cadherin, and inhibits the migration and invasion in KYSE150 and EC109 cells
malfunction
miR-BART1-5p directly targets GCNT3. In addition, miR-BART1-5p mimics transfection is observed to reduce cell proliferation and migration, while miR-BART1-5p inhibitor increases cell proliferation and migration following transfection. In conclusion, both miR-BART1-5p and knockdown of GCNT3 inhibit cell proliferation and migration
malfunction
talniflumate alone and in combination with low-dose gefitinib reduces GCNT3 expression, leading to the disrupted production of mucins in vivo and in vitro. Aberrant GCNT3 expression is associated with increased mucin production, aggressive tumorigenesis, and reduced patient survival. CRISPR-mediated knockout of GCNT3 in pancreatic cancer cells reduced proliferation and spheroid formation
metabolism
GCNT2 is a direct target of the TGF-beta-smad pathway and that change in GCNT2 expression modulates EMT induced by TGF-beta1 treatment. Involvement of GCNT2 in EMT and TGF-beta signaling, and further glycosylation modification of E-cadherin by GCNT2, are the underlying integrative mechanisms for breast cancer metastasis. GCNT2 contributes to distal metastasis in vivo
metabolism
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integrated transcriptomic and proteomic analyses reveal that GCNT3 is linked to cellular cycle, mitosis and proliferation, response to drugs and metabolism pathways. The vascular epithelial growth factor A (VEGFA) arises as an attractive partner of GCNT3 functions in cell invasion and resistance
physiological function
core 2 beta-1,6-N-acetylglucosaminyltransferase (GCNT3) is a core mucin-synthesizing enzyme. Correlations between GCNT3 expression and pancreatic tumor progression, Kaplan-Meier analysis of patients' survival by GCNT3 expression level, overview
physiological function
GCNT2 is a gene contributing to breast cancer metastasis with preferential expression in basal-like breast cancer. GCNT2 induces epithelial-mesenchymal transition and promotes migration and invasion in esophageal squamous cell carcinoma cells. Involvement of GCNT2 in the epithelial-to-mesenchymal transition (EMT). Specifically, the expression of E-cadherin is significantly changed upon GCNT2 expression at the protein level but not at the RNA level
physiological function
O-glycan synthase glucosamine (N-acetyl)transferase 3 (GCNT3) is a mucin-type responsible for catalyzing core 2 and core 4 O-glycans and forming O-linked glycosylation in protein biosynthesis. Abnormal expression of GCNT3 promotes the progression of several human cancers. GCNT3 expression in Epstein-Barr virus (EBV)-associated gastric cancer cells and tissues is lower than in EBV-negative gastric cancer cells and tissues, and high expression is significantly associated with advanced tumor-lymph node metastasis. EBV may regulate GCNT3 by affecting the NF-kappaB signaling pathway. Patients with EBV-associated gastric cancer (EBVaGC) have a good survival rate. EBV potentially regulates GCNT3 by affecting the NF-kappaB signaling pathway
physiological function
overall survival is significantly lower in esophageal squamous cell carcinoma patients with high GCNT2 expression than those with low GCNT2 expression
physiological function
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the mucin-type core 2 1,6-N-acetylglucosaminyltransferase enzyme (C2GnT-M), encoded by the GCNT3 gene, is a glycosyltransferase enzyme whose expression is altered in cancer processes. GCNT3 catalyzes the formation of core 2 O-glycan, core 4 O-glycan and I branches and its pattern of expression is mainly associated with colorectal cancer (CRC) prognosis. GCNT3 transfection in certain CRC cells reduces cell proliferation, adhesion, invasion, and induced cell death, and also inhibits tumor growth in vivo. Role of glycosyltransferase enzyme GCNT3 in colon and ovarian cancer prognosis and chemoresistance, overview. Integrated transcriptomic and proteomic analyses reveal that GCNT3 is linked to cellular cycle, mitosis and proliferation, response to drugs and metabolism pathways. GCNT3 overexpression contributes to reduce 5-fluorouracil resistance in metastatic CRC cells. GCNT3 also diminishes cell invasion and VEGFA expression in EOC cells. GCNT3 is a cancer prognostic factor. GCNT3 diminishes cell proliferation, invasion and alters metabolic properties of CRC cells. GCNT3 high-expressing Stage III-IV EOC patients have better response to conventional treatment and clinical outcome
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). GCNT3_HUMAN
438
1
50864
Swiss-Prot
Secretory Pathway (Reliability: 1)
GNT2A_HUMAN
402
1
45873
Swiss-Prot
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
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x * 67000-74000, glycosylated protein fused to glutathione S-transferase, size heterogenicity is at least partially due to differences in N-glycosylation, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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recombinant enzyme, expressed in SF9 insect cells as fusion protein with glutathione S-transferase has 5 potential N-glycosylation sites
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A169T
naturally occuring mutation in the GCNT2 gene causing blood group I and cataract formation phenotype
G310D
naturally occuring mutation in the GCNT2 gene causing blood group I and cataract formation phenotype
G334R
naturally occuring mutation in the GCNT2 gene causing blood group I and cataract formation phenotype
G348E
naturally occuring mutation in the GCNT2 gene causing blood group I and cataract formation phenotype
N388R
homozygous frameshift mutation c.1163_1166delATCA, p.(Asn388Argfs*20) is the cause of congenital cataract in two affected siblings, pleiotropic effect of the mutation causing congenital cataract and adult I blood group phenotype, overview
R226Q
naturally occuring mutation in the GCNT2 gene causing blood group I and cataract formation phenotype
R383H
naturally occuring mutation in the GCNT2 gene causing blood group I and cataract formation phenotype
W326stop
naturally occuring mutation in the GCNT2 gene causing blood group I and cataract formation phenotype
additional information
additional information
CRISPR-mediated knockout of GCNT3 in pancreatic cancer cells
additional information
-
GCNT3 downregulation by shGCNT3 7. GCNT3 overexpression reduces 5-fluorouracil resistance in colorectal cancer (CRC) cells. GCNT3 overexpression reduces proliferation, invasion and changes metabolic capacities of CRC cells. Genomic analysis of GCNT3 overexpression, overview
additional information
knockdown of GCNT3 using GCNT3-specific small interfering RNAs: siGCNT3-1 (GCUACUGCGAGCUGUGUAUTT), and siGCNT3-2 (GCUCAGUGCCGUGGAAAUATT). Reduction of the expression of endogenous GCNT3 by siRNA transfection in SGC7901 and BGC823 cells. Epstein-Barr virus (EBV) miRNA miR-BART1-5p specifically targets GCNT3. miR-BART1-5p suppresses GCNT3 expression, cell proliferation, and migration in EBVnGC, and the MiR-BART1-5p inhibitor increases GCNT3 expression, cell proliferation, and migration in transfected GT39 and GT38 cells. NF-kappaB can activate the expression of multiple miR-BARTs, including miR-BART1-5p
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of recombinant enzyme, expressed in SF9 insect cells as protein fused to glutathione S-transferase
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
C2GnT and IGnT cDNAs are cloned and sequenced, genes are both localized on chromosome 9, band q2l, genomic structures
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cotransfection and expression of Epstein-Barr virus (EBV) miRNA miR-BART1-5p and GCNT3 in HEK-293T and SGC7901 cells
gene GCNT3, recombinant overexpression in SW620 and SW5FU cell lines, genomic analysis of GCNT3 overexpression, quantitative RT-PCR enzyme expression analysis, genomic and proteomic landscapes of GCNT3 are linked to cell cycle and response to drug pathways. GCNT3 overexpression does not significantly change cell growth in Caov3 cells, VEGFA expression is downregulated in GCNT3 Caov3 cells
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IGnT6 is cloned, sequenced and cDNA encoding cIGnT6 in PA-1 cells is expressed in SF9 insect cells as protein fused to glutathione S-transferase
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
GCNT3 downregulation by shGCNT3 7, of several shRNAs targeting GCNT3 shGCNT3s, shGCNT3 7 has the best inhibitory capacity (protein and mRNA)
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modulation of GCNT3 expression in the presence of 5-fluorouracil (5FU) at 0.03 mM, a robust induction of GCNT3 expression is observed in SW family of non-resistant cells with a statistically significant 3.76fold increase in SW620 metastatic cells, while no such induction is observed in SW5FU cells or in HT-29 cell line, which has the highest levels of endogenous GCNT3
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talniflumate alone and in combination with low-dose gefitinib reduces GCNT3 expression, leading to the disrupted production of mucins in vivo and in vitro, in silico molecular docking studies. Talniflumate binds to GCNT3 with a docking affinity of -8.3 kcal/mol and deeper in the pocket of GCNT3. GALB1,3GALNAC's best docking affinity is -7.51 kcal/mol, achieved closer to the surface of GCNT3
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
medicine
GCNT2 is overexpressed in highly metastatic breast cancer and its expression correlates with adverse pathologic phenotypes. Blocking TGF-beta/GCNT2 signaling is a promising approach for targeting metastatic breast cancer
pharmacology
targeting mucin biosynthesis through GCNT3 may improve drug responsiveness
synthesis
-
cIGnT6 transfers multiple GlcNAc branches to long linear polylactosamines, a prerequisite for improving enzyme-assisted in vitro synthesis of a type of multivalent sialyl Lewis x glycans that are high affinity inhibitors of lymphocyte L-selectin, enzyme allows general polylactosamine synthesis
diagnostics
GCNT2 is a regulator of epithelial-mesenchymal transition (EMT) and a candidate prognostic indicator of outcome in esophageal squamous cell carcinoma (ESCC) patients
diagnostics
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GCNT3 might be an essential glycosylation-related molecule in colorectal cancer and epithelial ovarian cancer progression, with potential interest as a predictive biomarker of response to chemotherapy. GCNT3 high-expressing Stage III-IV EOC patients have better response to conventional treatment and clinical outcome. Clinical relevance of GCNT3 expression in epithelial ovarian cancer (EOC), role of GCNT3 as a biomarker for cancer patients, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Leppänen, A.; Penttilä, L.; Niemelä, R.; Helin, J.; Seppo, A.; Lusa, S.; Renkonen, O.
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Homo sapiens
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Homo sapiens
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Homo sapiens
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The centrally acting beta1,6N-acetylglucosaminyltransferase (GlcNAc to Gal). Functional expression, purification, and acceptor specificity of a human enzyme involved in midchain branching of linear poly-N-acetyllactosamines
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Homo sapiens
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Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
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Homo sapiens (Q8N0V5)
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Small-molecule inhibition of GCNT3 disrupts mucin biosynthesis and malignant cellular behaviors in pancreatic cancer
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Homo sapiens (O95395), Mus musculus (Q5JCT0), Mus musculus C5BL/6 (Q5JCT0)
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GCNT2 induces epithelial-mesenchymal transition and promotes migration and invasion in esophageal squamous cell carcinoma cells
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Homo sapiens (Q8N0V5), Homo sapiens
Cheong, S.S.; Hull, S.; Jones, B.; Chana, R.; Thornton, N.; Plagnol, V.; Moore, A.T.; Hardcastle, A.J.
Pleiotropic effect of a novel mutation in GCNT2 causing congenital cataract and a rare adult i blood group phenotype
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Homo sapiens (Q8N0V5)
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Homo sapiens
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