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Information on EC 2.4.1.244 - N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase and Organism(s) Homo sapiens and UniProt Accession Q76KP1
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2.4.1.244 N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferaseIUBMB Comments
The enzyme from human can transfer N-acetyl-D-galactosamine (GalNAc) to N-glycan and O-glycan substrates that have N-acetyl-D-glucosamine (GlcNAc) but not D-glucuronic acid (GlcUA) at their non-reducing end. The N-acetyl-beta-D-glucosaminyl group is normally on a core oligosaccharide although benzyl glycosides have been used in enzyme-characterization experiments. Some glycohormones, e.g. lutropin and thyrotropin contain the N-glycan structure containing the N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl group.
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Word Map
- 2.4.1.244
- lacdinac
- o-glycans
- n-acetylgalactosamine
- glycosyltransferases
- floribunda
- agglutinin
- wisteria
- glcnac
- paxillin
-
mucin-type
-
biobanks
- glycosphingolipids
-
brainiac
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
b4galnt3, beta4galnac-t3, beta4galnactb, beta1,4-n-acetylgalactosaminyltransferase iii, beta1,4-n-acetylgalactosaminyltransferase-iii, beta4galnac-t4, beta1,4-n-acetylgalactosaminyltransferase ii, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 1
-
beta1,4-N-acetylgalactosaminyltransferase III
beta4GalNAc-T3
N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 2
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-galactosamine:N-acetyl-beta-D-glucosaminyl-group 4-beta-N-acetylgalactosaminyltransferase
The enzyme from human can transfer N-acetyl-D-galactosamine (GalNAc) to N-glycan and O-glycan substrates that have N-acetyl-D-glucosamine (GlcNAc) but not D-glucuronic acid (GlcUA) at their non-reducing end. The N-acetyl-beta-D-glucosaminyl group is normally on a core oligosaccharide although benzyl glycosides have been used in enzyme-characterization experiments. Some glycohormones, e.g. lutropin and thyrotropin contain the N-glycan structure containing the N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl group.
CAS REGISTRY NUMBER
COMMENTARY
163913-55-1
-
67338-98-1
-
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-GalNAc + Gal-beta-(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
UDP + Gal-beta-(1,4)-GalNAc-beta(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
26.2% of the activity with GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
-
-
?
UDP-GalNAc + Gal-beta-(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-[Fuc-alpha-(1,6)]-GlcNAc-2-pyridylaminoside
UDP + GalNAc-beta(1,4)-Gal-beta-(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-[Fuc-alpha-(1,6)]-GlcNAc-2-pyridylaminoside
26.7% of the activity with GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
-
-
?
UDP-GalNAc + GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[Gal-beta-(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
UDP + GalNAc-beta(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[Gal-beta-(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
16.2% of the activity with GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
-
-
?
UDP-GalNAc + GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[Gal-beta-(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-[Fuc-alpha-(1,6)]-GlcNAc-2-pyridylaminoside
UDP + GalNAc-beta(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[Gal-beta-(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-[Fuc-alpha-(1,6)]-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
3.4% of the activity with GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
-
-
?
UDP-GalNAc + GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
UDP + GalNAc-beta(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
-
-
-
?
UDP-GalNAc + GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-[Fuc-alpha-(1,6)]-GlcNAc-2-pyridylaminoside
UDP + GalNAc-beta(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
76.8% of the activity with GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
-
-
?
UDP-GalNAc + GlcNAc-beta-(1,3)-GalNAc-alpha-p-nitrophenyl
UDP + GalNAc-beta-(1,4)-GlcNAc-beta-(1,3)-GalNAc-alpha-p-nitrophenyl
20.0% of the activity with GlcNAcbeta-O-benzyl
-
-
?
UDP-GalNAc + GlcNAc-beta-(1,6)-GalNAc-alpha-p-nitrophenyl
UDP + GalNAc-beta-(1,4)-GlcNAc-beta-(1,6)-GalNAc-alpha-p-nitrophenyl
190.7% of the activity with GlcNAcbeta-O-benzyl
-
-
?
UDP-GalNAc + GlcNAc-beta-(1,6)[Gal-beta-(1,3)]GalNAc-alpha-p-nitrophenyl
UDP + GalNAc-beta-(1,4)-GlcNAc-beta-(1,6)[Gal-beta-(1,3)]GalNAc-alpha-p-nitrophenyl
15.2% of the activity with GlcNAcbeta-O-benzyl
-
-
?
UDP-GalNAc + GlcNAcbeta-O-benzyl
UDP + GalNAc-beta-(1,4)-GlcNAcbeta-O-benzyl
-
-
-
?
UDP-GalNAc + Gal-beta-(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
UDP + Gal-beta-(1,4)-GalNAc-beta(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
45% of the activity with GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
-
-
?
UDP-GalNAc + Gal-beta-(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-[Fuc-alpha-(1,6)]-GlcNAc-2-pyridylaminoside
UDP + GalNAc-beta(1,4)-Gal-beta-(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-[Fuc-alpha-(1,6)]-GlcNAc-2-pyridylaminoside
51.7% of the activity with GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
-
-
?
UDP-GalNAc + GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[Gal-beta-(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
UDP + GalNAc-beta(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[Gal-beta-(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
21.6% of the activity with GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
-
-
?
UDP-GalNAc + GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[Gal-beta-(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-[Fuc-alpha-(1,6)]-GlcNAc-2-pyridylaminoside
UDP + GalNAc-beta(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[Gal-beta-(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-[Fuc-alpha-(1,6)]-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
5% of the activity with GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
-
-
?
UDP-GalNAc + GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
UDP + GalNAc-beta(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
-
-
-
?
UDP-GalNAc + GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-[Fuc-alpha-(1,6)]-GlcNAc-2-pyridylaminoside
UDP + GalNAc-beta(1,4)-GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
87.1% of the activity with GlcNAc-beta-(1,2)-Man-alpha-(1,6)-[GlcNAc-beta-(1,2)-Man-alpha-(1,3)]Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc-2-pyridylaminoside
-
-
?
UDP-GalNAc + GlcNAc-beta-(1,3)-GalNAc-alpha-p-nitrophenyl
UDP + GalNAc-beta-(1,4)-GlcNAc-beta-(1,3)-GalNAc-alpha-p-nitrophenyl
-
-
-
-
?
UDP-GalNAc + GlcNAcbeta-O-benzyl
UDP + GalNAc-beta-(1,4)-GlcNAcbeta-O-benzyl
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + N-acetyl-beta-D-glucosamine
UDP + N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosamine
enzyme B4GALNT3 transfers N-acetylgalactosamine (GalNAc) to the non-reducing N-acetylglucosamine (GlcNAc) to form GalNAcbeta1-4GlcNAc (LacdiNAc) in an in vitro enzymatic assay
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + N-acetyl-beta-D-glucosaminyl group
UDP + N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl group
-
-
-
?
additional information
?
-
the enzyme mediates the protein-specific addition of beta1,4-linked GalNAc to core 2 O-linked structures both in vivo and in vitro
-
-
?
additional information
?
-
the enzyme could transfer GalNAc residues, producing N,N'-diacetylgalactosediamine structures at least in N-glycans and probably in both N- and O-glycans
-
-
?
additional information
?
-
-
the enzyme could transfer GalNAc residues, producing N,N'-diacetylgalactosediamine structures at least in N-glycans and probably in both N- and O-glycans
-
-
?
additional information
?
-
the most efficient acceptor substrate in the N-glycans examined is a non-fucosylated bi-antennary one. The enzyme shows no activity towards chondroitin-related acceptors containing GlcUA as their non-reducing termini
-
-
?
additional information
?
-
-
the most efficient acceptor substrate in the N-glycans examined is a non-fucosylated bi-antennary one. The enzyme shows no activity towards chondroitin-related acceptors containing GlcUA as their non-reducing termini
-
-
?
additional information
?
-
enzyme B4GALNT3 primarily modifies N-glycans of epithelial growth factor receptor, EGFR, in LacdiNAc by Wisteria floribunda agglutinin pull down assays
-
-
?
additional information
?
-
-
enzyme B4GALNT3 primarily modifies N-glycans of epithelial growth factor receptor, EGFR, in LacdiNAc by Wisteria floribunda agglutinin pull down assays
-
-
?
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
additional information
?
-
the enzyme could transfer GalNAc residues, producing N,N'-diacetylgalactosediamine structures at least in N-glycans and probably in both N- and O-glycans
-
-
?
additional information
?
-
-
the enzyme could transfer GalNAc residues, producing N,N'-diacetylgalactosediamine structures at least in N-glycans and probably in both N- and O-glycans
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
beta4GalNAcT-II acts as a negative regulator of carbohydrate determinant sialyl Lewis x expression in colon cancer
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
primary, B4GALNT3 expression in different stage of colorectal tumors, overview
high enzyme expression level in epithelial cells of gastric mucosa
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
apical Golgi localization. The supra-nuclear expression of the enzyme is essential for the formation of GalNAC-beta-(1,4)-GlcNAc on the surface of mucous cells
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
B4GALNT3 overexpression enhances colon cancer cell malignant phenotypes in vitro and in vivo. B4GALNT3 knockdown suppresses EGF-induced phosphorylation of epithelial growth factor receptor, EGFR, and its downstream signaling molecules. B4GALNT3 knockdown inhibits EGFR activity, decreases EGF-induced migration and invasion in colon cancer cells, and promotes EGFR degradation in colon cancer cells, overview
physiological function
beta1,4-N-acetylgalactosaminyltransferase III modulates cancer stemness through EGFR signaling pathway in colon cancer cells, B4GALNT3 regulates cancer stemness and the invasive properties of colon cancer cells through modifying EGFR glycosylation and signaling. B4GALNT3 expression is positively correlated with advanced stages and poor survival in colorectal cancer patients
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). B4GN4_HUMAN
1039
1
116513
Swiss-Prot
Secretory Pathway (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
B4GALNT3 overexpression enhances colon cancer cell malignant phenotypes in vitro and in vivo. Knockdown of B4GALNT3 using small interfering (si) RNAs in colon cancer cell lines (HCT116, SW480, HCT15, and HT29 cells) decrease sphere formation and the expression of stem cell markers, OCT4 and. NANOG. B4GALNT3 knockdown suppresses EGF-induced phosphorylation of epithelial growth factor receptor, EGFR, and its downstream signaling molecules
additional information
-
B4GALNT3 overexpression enhances colon cancer cell malignant phenotypes in vitro and in vivo. Knockdown of B4GALNT3 using small interfering (si) RNAs in colon cancer cell lines (HCT116, SW480, HCT15, and HT29 cells) decrease sphere formation and the expression of stem cell markers, OCT4 and. NANOG. B4GALNT3 knockdown suppresses EGF-induced phosphorylation of epithelial growth factor receptor, EGFR, and its downstream signaling molecules
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the putative catalytic domain of beta4GalNAc-T4 is expressed as a secreted protein fused with a FLAG peptide in HEK293T cells
truncated form of the human enzyme is expressed in HEK293T cells as a soluble protein
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
GalNAC-beta-(1,4)-GlcNAc and beta4GalNAc-T3 are novel differentiation markers of surface mucous cells in the gastric mucosa
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gotoh, M.; Sato, T.; Kiyohara, K.; Kameyama, A.; Kikuchi, N.; Kwon, Y.D.; Ishizuka, Y.; Iwai, T.; Nakanishi, H.; Narimatsu, H.
Molecular cloning and characterization of beta1,4-N-acetylgalactosaminyltransferases IV synthesizing N,N'-diacetyllactosediamine
FEBS Lett.
562
134-140
2004
Homo sapiens (Q76KP1), Homo sapiens
Ikehara, Y.; Sato, T.; Nakamura, S.; Gotoh, M.; Ikehara, S.K.; Kiyohara, K.; Aoki, C.; Iwai, T.; Nakanishi, H.; Hirabayashi, J.; Tatematsu, M.; Narimatsu, H.
Apical Golgi localization of N,N'-diacetyllactosediamine synthase, beta4GalNAc-T3, is responsible for LacdiNAc expression on gastric mucosa
Glycobiology
16
777-785
2006
Homo sapiens
Sato, T.; Gotoh, M.; Kiyohara, K.; Kameyama, A.; Kubota, T.; Kikuchi, N.; Ishizuka, Y.; Iwasaki, H.; Togayachi, A.; Kudo, T.; Ohkura, T.; Nakanishi, H.; Narimatsu, H.
Molecular cloning and characterization of a novel human beta1,4-N-acetylgalactosaminyltransferase, beta4GalNAc-T3, responsible for the synthesis of N,N'-diacetyllactosediamine, GalNAc beta1-4GlcNAc
J. Biol. Chem.
278
47534-47544
2003
Homo sapiens (Q6L9W6), Homo sapiens
Malagolini, N.; Santini, D.; Chiricolo, M.; DallOlio, F.
Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon
Glycobiology
17
688-697
2007
Homo sapiens
Huang, J.; Liang, J.T.; Huang, H.C.; Shen, T.L.; Chen, H.Y.; Lin, N.Y.; Che, M.I.; Lin, W.C.; Huang, M.C.
Beta1,4-N-acetylgalactosaminyltransferase III enhances malignant phenotypes of colon cancer cells
Mol. Cancer Res.
5
543-552
2007
Homo sapiens
Fiete, D.; Beranek, M.; Baenziger, J.U.
Peptide-specific transfer of N-acetylgalactosamine to O-linked glycans by the glycosyltransferases beta1,4-N-acetylgalactosaminyl transferase 3 (beta4GalNAc-T3) and beta4GalNAc-T4
J. Biol. Chem.
287
29204-29212
2012
Homo sapiens (Q76KP1)
Che, M.I.; Huang, J.; Hung, J.S.; Lin, Y.C.; Huang, M.J.; Lai, H.S.; Hsu, W.M.; Liang, J.T.; Huang, M.C.
beta1,4-N-acetylgalactosaminyltransferase III modulates cancer stemness through EGFR signaling pathway in colon cancer cells
Oncotarget
5
3673-3684
2014
Homo sapiens (Q6L9W6), Homo sapiens
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