GCNT1

GCNT1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2GAK, 2GAM, 3OTK
Identifiers
Aliases	GCNT1 , C2GNT, C2GNT-L, C2GNT1, G6NT, NACGT2, NAGCT2, glucosaminyl (N-acetyl) transferase 1, core 2, glucosaminyl (N-acetyl) transferase 1
External IDs	OMIM: 600391 MGI: 95676 HomoloGene: 37486 GeneCards: GCNT1
Gene location (Human)
Chr.	Chromosome 9 (human)
End	76,651,203 bp
Gene location (Mouse)
Chr.	Chromosome 19 (mouse)
End	17,350,208 bp
RNA expression pattern
	Top expressed in
	duodenum; ; jejunal mucosa; ; islet of Langerhans; ; amniotic fluid; ; Achilles tendon; ; secondary oocyte; ; rectum; ; monocyte; ; stomach; ; right lobe of thyroid gland;
	Top expressed in
	parotid gland; ; proximal tubule; ; kidney; ; atrioventricular valve; ; left colon; ; aortic valve; ; blood; ; urothelium; ; hair follicle; ; proximal convoluted tubule;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity ; acetylglucosaminyltransferase activity ; glycosyltransferase activity ; beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity ; protein binding ;
Cellular component	integral component of membrane ; Golgi apparatus ; membrane ; Golgi cisterna ; trans-Golgi network ; Golgi membrane ; extracellular space ;
Biological process	glycoprotein biosynthetic process ; tissue morphogenesis ; response to insulin ; protein glycosylation ; kidney morphogenesis ; O-glycan processing ; leukocyte tethering or rolling ; cell adhesion molecule production ;
	Sources:Amigo / QuickGO
Orthologs
	2650
	14537
	ENSG00000187210
	ENSMUSG00000038843
	Q02742
	Q09324
	NM_001097633 ; NM_001097634 ; NM_001097635 ; NM_001097636 ; NM_001490
	NM_001136484 ; NM_010265 ; NM_173442
	NP_001091102 ; NP_001091103 ; NP_001091104 ; NP_001091105 ; NP_001481
	NP_001129956 ; NP_034395 ; NP_775618
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 14, 2022

Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the GCNT1 gene.^[5]^[6]^[7]

This gene is a member of the beta-1,6-N-acetylglucosaminyltransferase gene family. It is essential to the formation of Gal beta 1-3(GlcNAc beta 1-6)GalNAc structures and the core 2 O-glycan branch. The gene coding this enzyme was originally mapped to 9q21, but was later localized to 9q13. Multiple alternatively spliced variants, encoding the same protein, have been identified.^[7]

Related Research Articles

The enzyme UDP-glucose 4-epimerase, also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.

Beta-1,4-galactosyltransferase 1 is an enzyme that in humans is encoded by the B4GALT1 gene.

Carbohydrate sulfotransferase 6 is an enzyme that in humans is encoded by the CHST6 gene.

Alpha-(1,3)-fucosyltransferase is an enzyme that in humans is encoded by the FUT7 gene.

N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase is an enzyme that in humans is encoded by the GCNT2 gene.

UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme that in humans is encoded by the DPAGT1 gene.

Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the MGAT3 gene.

Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A is an enzyme that in humans is encoded by the MGAT5 gene.

Carbohydrate sulfotransferase 4 is an enzyme that in humans is encoded by the CHST4 gene.

CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase is an enzyme that in humans is encoded by the ST3GAL4 gene.

UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 is an enzyme that in humans is encoded by the B3GNT2 gene.

UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3 is an enzyme that in humans is encoded by the B3GNT3 gene.

Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the MGAT1 gene.

Beta-1,4-galactosyltransferase 2 is an enzyme that in humans is encoded by the B4GALT2 gene.

Beta-1,4-galactosyltransferase 5 is an enzyme that in humans is encoded by the B4GALT5 gene.

Carbohydrate sulfotransferase 5 is an enzyme that in humans is encoded by the CHST5 gene.

Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2 is an enzyme that in humans is encoded by the B3GAT2 gene.

Beta-1,4-galactosyltransferase 4 is an enzyme that in humans is encoded by the B4GALT4 gene.

Beta-1,4-galactosyltransferase 3 is an enzyme that in humans is encoded by the B4GALT3 gene.

O-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O-glycosylation is a post-translational modification that occurs after the protein has been synthesised. In eukaryotes, it occurs in the endoplasmic reticulum, Golgi apparatus and occasionally in the cytoplasm; in prokaryotes, it occurs in the cytoplasm. Several different sugars can be added to the serine or threonine, and they affect the protein in different ways by changing protein stability and regulating protein activity. O-glycans, which are the sugars added to the serine or threonine, have numerous functions throughout the body, including trafficking of cells in the immune system, allowing recognition of foreign material, controlling cell metabolism and providing cartilage and tendon flexibility. Because of the many functions they have, changes in O-glycosylation are important in many diseases including cancer, diabetes and Alzheimer's. O-glycosylation occurs in all domains of life, including eukaryotes, archaea and a number of pathogenic bacteria including Burkholderia cenocepacia, Neisseria gonorrhoeae and Acinetobacter baumannii.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000187210 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000038843 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Bierhuizen MF, Mattei MG, Fukuda M (Apr 1993). "Expression of the developmental I antigen by a cloned human cDNA encoding a member of a beta-1,6-N-acetylglucosaminyltransferase gene family". Genes Dev. 7 (3): 468–78. doi: 10.1101/gad.7.3.468 . PMID 8449405.
↑ Yeh JC, Ong E, Fukuda M (Mar 1999). "Molecular cloning and expression of a novel beta-1, 6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches". J Biol Chem. 274 (5): 3215–21. doi: 10.1074/jbc.274.5.3215 . PMID 9915862.
1 2 "Entrez Gene: GCNT1 glucosaminyl (N-acetyl) transferase 1, core 2 (beta-1,6-N-acetylglucosaminyltransferase)".

Bierhuizen MF, Fukuda M (1992). "Expression cloning of a cDNA encoding UDP-GlcNAc:Gal beta 1-3-GalNAc-R (GlcNAc to GalNAc) beta 1-6GlcNAc transferase by gene transfer into CHO cells expressing polyoma large tumor antigen". Proc. Natl. Acad. Sci. U.S.A. 89 (19): 9326–330. Bibcode:1992PNAS...89.9326B. doi: 10.1073/pnas.89.19.9326 . PMC 50119 . PMID 1329093.
Bierhuizen MF, Maemura K, Kudo S, Fukuda M (1995). "Genomic organization of core 2 and I branching beta-1,6-N-acetylglucosaminyltransferases. Implication for evolution of the beta-1,6-N-acetylglucosaminyltransferase gene family". Glycobiology. 5 (4): 417–25. doi:10.1093/glycob/5.4.417. PMID 7579796.
Skrincosky D, Kain R, El-Battari A, et al. (1997). "Altered Golgi localization of core 2 beta-1,6-N-acetylglucosaminyltransferase leads to decreased synthesis of branched O-glycans". J. Biol. Chem. 272 (36): 22695–702. doi: 10.1074/jbc.272.36.22695 . PMID 9278427.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Beum PV, Bastola DR, Cheng PW (2003). "Mucin biosynthesis: epidermal growth factor downregulates core 2 enzymes in a human airway adenocarcinoma cell line". Am. J. Respir. Cell Mol. Biol. 29 (1): 48–56. doi:10.1165/rcmb.2002-0147OC. PMID 12600830.
Falkenberg VR, Alvarez K, Roman C, Fregien N (2004). "Multiple transcription initiation and alternative splicing in the 5' untranslated region of the core 2 beta1-6 N-acetylglucosaminyltransferase I gene". Glycobiology. 13 (6): 411–8. doi: 10.1093/glycob/cwg039 . PMID 12626388.
Chibber R, Ben-Mahmud BM, Mann GE, et al. (2003). "Protein kinase C beta2-dependent phosphorylation of core 2 GlcNAc-T promotes leukocyte-endothelial cell adhesion: a mechanism underlying capillary occlusion in diabetic retinopathy". Diabetes. 52 (6): 1519–27. doi: 10.2337/diabetes.52.6.1519 . PMID 12765965.
Smith MJ, Smith BR, Lawrence MB, Snapp KR (2004). "Functional analysis of the combined role of the O-linked branching enzyme core 2 beta1-6-N-glucosaminyltransferase and dimerization of P-selectin glycoprotein ligand-1 in rolling on P-selectin". J. Biol. Chem. 279 (21): 21984–91. doi: 10.1074/jbc.M402731200 . PMID 15026421.
Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316 . PMID 15342556.
Kikuchi J, Shinohara H, Nonomura C, et al. (2005). "Not core 2 beta 1,6-N-acetylglucosaminyltransferase-2 or -3 but -1 regulates sialyl-Lewis x expression in human precursor B cells". Glycobiology. 15 (3): 271–80. doi: 10.1093/glycob/cwi005 . PMID 15483269.
Beum PV, Basma H, Bastola DR, Cheng PW (2005). "Mucin biosynthesis: upregulation of core 2 beta 1,6 N-acetylglucosaminyltransferase by retinoic acid and Th2 cytokines in a human airway epithelial cell line". Am. J. Physiol. Lung Cell Mol. Physiol. 288 (1): L116–24. doi:10.1152/ajplung.00370.2003. PMID 15591039.
Wang L, Mitoma J, Tsuchiya N, et al. (2005). "An A/G polymorphism of core 2 branching enzyme gene is associated with prostate cancer". Biochem. Biophys. Res. Commun. 331 (4): 958–63. doi:10.1016/j.bbrc.2005.04.022. PMID 15882971.
Prorok-Hamon M, Notel F, Mathieu S, et al. (2006). "N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding". Biochem. J. 391 (Pt 3): 491–502. doi:10.1042/BJ20050344. PMC 1276950 . PMID 15926890.
Hagisawa S, Ohyama C, Takahashi T, et al. (2006). "Expression of core 2 beta1,6-N-acetylglucosaminyltransferase facilitates prostate cancer progression". Glycobiology. 15 (10): 1016–24. doi: 10.1093/glycob/cwi086 . PMID 15932919.
Kikuchi J, Ozaki H, Nonomura C, et al. (2005). "Transfection of antisense core 2 beta1,6-N-acetylglucosaminyltransferase-1 cDNA suppresses selectin ligand expression and tissue infiltration of B-cell precursor leukemia cells". Leukemia. 19 (11): 1934–40. doi: 10.1038/sj.leu.2403951 . PMID 16179912.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129 . PMID 16344560.
Cabrera PV, Amano M, Mitoma J, et al. (2006). "Haploinsufficiency of C2GnT-I glycosyltransferase renders T lymphoma cells resistant to cell death". Blood. 108 (7): 2399–406. doi:10.1182/blood-2006-04-018556. PMC 1895562 . PMID 16778138.
Julien S, Grimshaw MJ, Sutton-Smith M, et al. (2007). "Sialyl-Lewis(x) on P-selectin glycoprotein ligand-1 is regulated during differentiation and maturation of dendritic cells: a mechanism involving the glycosyltransferases C2GnT1 and ST3Gal I." J. Immunol. 179 (9): 5701–10. doi: 10.4049/jimmunol.179.9.5701 . PMID 17947642.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000187210 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000038843 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8449405-5] Bierhuizen MF, Mattei MG, Fukuda M (Apr 1993). "Expression of the developmental I antigen by a cloned human cDNA encoding a member of a beta-1,6-N-acetylglucosaminyltransferase gene family". Genes Dev. 7 (3): 468–78. doi: 10.1101/gad.7.3.468 . PMID 8449405.

[pmid9915862-6] Yeh JC, Ong E, Fukuda M (Mar 1999). "Molecular cloning and expression of a novel beta-1, 6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches". J Biol Chem. 274 (5): 3215–21. doi: 10.1074/jbc.274.5.3215 . PMID 9915862.

[entrez-7] 1 2 "Entrez Gene: GCNT1 glucosaminyl (N-acetyl) transferase 1, core 2 (beta-1,6-N-acetylglucosaminyltransferase)".

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GCNT1

Related Research Articles

References

Further reading