GALNT3

GALNT3
Identifiers
Aliases	GALNT3 , GalNAc-T3, HFTC, HHS, polypeptide N-acetylgalactosaminyltransferase 3, HFTC1
External IDs	OMIM: 601756 MGI: 894695 HomoloGene: 55827 GeneCards: GALNT3
Gene location (Human)
Chr.	Chromosome 2 (human)
End	165,794,659 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	65,955,338 bp
RNA expression pattern
	Top expressed in
	bronchial epithelial cell; ; parotid gland; ; jejunal mucosa; ; rectum; ; palpebral conjunctiva; ; pylorus; ; right uterine tube; ; duodenum; ; islet of Langerhans; ; cavity of mouth;
	Top expressed in
	parotid gland; ; lacrimal gland; ; submandibular gland; ; spermatocyte; ; spermatid; ; seminiferous tubule; ; conjunctival fornix; ; epithelium of stomach; ; mucous cell of stomach; ; calvaria;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	transferase activity ; calcium ion binding ; manganese ion binding ; glycosyltransferase activity ; metal ion binding ; polypeptide N-acetylgalactosaminyltransferase activity ; protein binding ; carbohydrate binding ;
Cellular component	integral component of membrane ; Golgi apparatus ; membrane ; Golgi membrane ; Golgi cisterna membrane ; perinuclear region of cytoplasm ; extracellular exosome ;
Biological process	protein O-linked glycosylation via serine ; protein glycosylation ; protein O-linked glycosylation via threonine ; O-glycan processing ; fibroblast growth factor receptor signaling pathway ; carbohydrate metabolic process ;
	Sources:Amigo / QuickGO
Orthologs
	2591
	14425
	ENSG00000115339
	ENSMUSG00000026994
	Q14435
	P70419
	NM_004482
	NM_015736
	NP_004473
	NP_056551
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated August 13, 2023

Polypeptide N-acetylgalactosaminyltransferase 3 is an enzyme that in humans is encoded by the GALNT3 gene.^[5]^[6]^[7]

This gene encodes UDP-GalNAc transferase 3, a member of the polypeptide GalNAc transferase (GalNAc-T) family. This family transfers an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O-linked oligosaccharide biosynthesis. Individual GalNAc-transferases have distinct activities and initiation of O-glycosylation is regulated by a repertoire of GalNAc-transferases. The protein encoded by this gene is highly homologous to other family members; however, the enzymes have different substrate specificities.^[7]

Related Research Articles

In enzymology, a globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a polypeptide N-acetylgalactosaminyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase is an enzyme that catalyzes the chemical reaction

Polypeptide N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the GALNT1 gene.

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

Polypeptide N-acetylgalactosaminyltransferase 2 is an enzyme that in humans is encoded by the GALNT2 gene.

UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the B3GALNT1 gene.

Beta-1,4 N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the B4GALNT1 gene.

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

Polypeptide N-acetylgalactosaminyltransferase 6 is an enzyme that in humans is encoded by the GALNT6 gene.

Polypeptide N-acetylgalactosaminyltransferase 13 is an enzyme that in humans is encoded by the GALNT13 gene.

Polypeptide N-acetylgalactosaminyltransferase 11 is an enzyme that in humans is encoded by the GALNT11 gene.

Histo-blood group ABO system transferase is an enzyme with glycosyltransferase activity, which is encoded by the ABO gene in humans. It is ubiquitously expressed in many tissues and cell types. ABO determines the ABO blood group of an individual by modifying the oligosaccharides on cell surface glycoproteins. Variations in the sequence of the protein between individuals determine the type of modification and the blood group. The ABO gene also contains one of 27 SNPs associated with increased risk of coronary artery disease.

Beta-1,4 N-acetylgalactosaminyltransferase 2 is an enzyme that in humans is encoded by the B4GALNT2 gene.

Polypeptide N-acetylgalactosaminyltransferase 14 is an enzyme that in humans is encoded by the GALNT14 gene.

(N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-galactosamine:1-O-(O- - -O-beta-D-galactopyranosyl- -beta-D-glucopyranosyl)-ceramide 4-beta-N-acetyl-D-galactosaminyltransferase. This enzyme catalyses the following chemical reaction

Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase (EC 2.4.1.148 with systematic name UDP-N-acetyl-D-glucosamine:N-acetyl-beta-D-glucosaminyl- -N-acetyl-D-galactosaminyl-R 6-beta-N-acetyl-D-glucosaminyltransferase. This enzyme catalyses the following chemical reaction

N-acetylneuraminylgalactosylglucosylceramide beta-1,4-N-acetylgalactosaminyltransferase (EC 2.4.1.165, is an enzyme that catalyses the following chemical reaction:

Protein O-GlcNAc transferase also known as OGT or O-linked N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the OGT gene. OGT catalyzes the addition of the O-GlcNAc post-translational modification to proteins.

N-acetylgalactosamine-N, N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-alpha-N-acetylgalactosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-galactosamine:N-acetylgalactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol 3-alpha-N-acetyl-D-galactosaminyltransferase. This enzyme catalyses the following chemical reaction

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000115339 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026994 - 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.
↑ Bennett EP, Weghuis DO, Merkx G, van Kessel AG, Eiberg H, Clausen H (Jul 1998). "Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family". Glycobiology. 8 (6): 547–55. doi: 10.1093/glycob/8.6.547 . PMID 9592121.
↑ Topaz O, Shurman DL, Bergman R, Indelman M, Ratajczak P, Mizrachi M, Khamaysi Z, Behar D, Petronius D, Friedman V, Zelikovic I, Raimer S, Metzker A, Richard G, Sprecher E (May 2004). "Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis". Nat Genet. 36 (6): 579–81. doi: 10.1038/ng1358 . PMID 15133511.
1 2 "Entrez Gene: GALNT3 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 3 (GalNAc-T3)".

Bennett EP, Hassan H, Clausen H (1996). "cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3". J. Biol. Chem. 271 (29): 17006–12. doi: 10.1074/jbc.271.29.17006 . PMID 8663203.
Wandall HH, Hassan H, Mirgorodskaya E, et al. (1997). "Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3". J. Biol. Chem. 272 (38): 23503–14. doi: 10.1074/jbc.272.38.23503 . PMID 9295285.
Röttger S, White J, Wandall HH, et al. (1998). "Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus". J. Cell Sci. 111 (1): 45–60. doi:10.1242/jcs.111.1.45. PMID 9394011.
Mandel U, Hassan H, Therkildsen MH, et al. (1999). "Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family". Glycobiology. 9 (1): 43–52. doi: 10.1093/glycob/9.1.43 . PMID 9884405.
Dosaka-Akita H, Kinoshita I, Yamazaki K, et al. (2002). "N-acetylgalactosaminyl transferase-3 is a potential new marker for non-small cell lung cancers". Br. J. Cancer. 87 (7): 751–5. doi:10.1038/sj.bjc.6600536. PMC 2364253 . PMID 12232759.
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.
Argüeso P, Tisdale A, Mandel U, et al. (2003). "The cell-layer- and cell-type-specific distribution of GalNAc-transferases in the ocular surface epithelia is altered during keratinization". Invest. Ophthalmol. Vis. Sci. 44 (1): 86–92. doi: 10.1167/iovs.02-0181 . PMID 12506059.
Onitsuka K, Shibao K, Nakayama Y, et al. (2003). "Prognostic significance of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-3 (GalNAc-T3) expression in patients with gastric carcinoma". Cancer Sci. 94 (1): 32–6. doi: 10.1111/j.1349-7006.2003.tb01348.x . PMID 12708471. S2CID 42340701.
Yamamoto S, Nakamori S, Tsujie M, et al. (2004). "Expression of uridine diphosphate N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyl transferase 3 in adenocarcinoma of the pancreas". Pathobiology. 71 (1): 12–8. doi:10.1159/000072957. PMID 14555840. S2CID 20321446.
Gu C, Oyama T, Osaki T, et al. (2004). "Low expression of polypeptide GalNAc N-acetylgalactosaminyl transferase-3 in lung adenocarcinoma: impact on poor prognosis and early recurrence". Br. J. Cancer. 90 (2): 436–42. doi:10.1038/sj.bjc.6601531. PMC 2409559 . PMID 14735190.
Miyahara N, Shoda J, Kawamoto T, et al. (2004). "Expression of UDP-N-acetyl-alpha-D-galactosamine-polypeptide N-acetylgalactosaminyltransferase isozyme 3 in the subserosal layer correlates with postsurgical survival of pathological tumor stage 2 carcinoma of the gallbladder". Clin. Cancer Res. 10 (6): 2090–9. doi: 10.1158/1078-0432.CCR-1024-03 . PMID 15041730.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
Ishikawa M, Kitayama J, Kohno K, Nagawa H (2005). "The expression pattern of UDP-N-acetyl-alpha-D-galactosamine-polypeptide N-acetyl-galactosaminyl transferase-3 in squamous cell carcinoma of the esophagus". Pathobiology. 72 (3): 139–45. doi:10.1159/000084117. PMID 15860931. S2CID 33360750.
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.
Kato K, Jeanneau C, Tarp MA, et al. (2006). "Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation". J. Biol. Chem. 281 (27): 18370–7. doi: 10.1074/jbc.M602469200 . PMID 16638743.
Ichikawa S, Imel EA, Sorenson AH, et al. (2007). "Tumoral calcinosis presenting with eyelid calcifications due to novel missense mutations in the glycosyl transferase domain of the GALNT3 gene". J. Clin. Endocrinol. Metab. 91 (11): 4472–5. doi: 10.1210/jc.2006-1247 . PMID 16940445.
Barbieri AM, Filopanti M, Bua G, Beck-Peccoz P (2007). "Two novel nonsense mutations in GALNT3 gene are responsible for familial tumoral calcinosis". J. Hum. Genet. 52 (5): 464–8. doi: 10.1007/s10038-007-0126-5 . PMID 17351710.
Inoue T, Eguchi T, Oda Y, et al. (2007). "Expression of GalNAc-T3 and its relationships with clinicopathological factors in 61 extrahepatic bile duct carcinomas analyzed using stepwise sections - special reference to its association with lymph node metastases-". Mod. Pathol. 20 (2): 267–76. doi: 10.1038/modpathol.3800700 . PMID 17361208.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000115339 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026994 - 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.

[pmid9592121-5] Bennett EP, Weghuis DO, Merkx G, van Kessel AG, Eiberg H, Clausen H (Jul 1998). "Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family". Glycobiology. 8 (6): 547–55. doi: 10.1093/glycob/8.6.547 . PMID 9592121.

[pmid15133511-6] Topaz O, Shurman DL, Bergman R, Indelman M, Ratajczak P, Mizrachi M, Khamaysi Z, Behar D, Petronius D, Friedman V, Zelikovic I, Raimer S, Metzker A, Richard G, Sprecher E (May 2004). "Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis". Nat Genet. 36 (6): 579–81. doi: 10.1038/ng1358 . PMID 15133511.

[entrez-7] 1 2 "Entrez Gene: GALNT3 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 3 (GalNAc-T3)".

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GALNT3

Related Research Articles

References

Further reading