GALNT3

Identifiers

GALNT3, GalNAc-T3, HFTC, HHS, polypeptide N-acetylgalactosaminyltransferase 3

External IDs

MGI: 894695 HomoloGene: 55827 GeneCards: GALNT3

Gene ontology
Molecular function	• transferase activity • calcium ion binding • manganese ion binding • transferase activity, transferring glycosyl groups • 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 • carbohydrate metabolic process • protein glycosylation • protein O-linked glycosylation via threonine • O-glycan processing • fibroblast growth factor receptor signaling pathway
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


2591


14425

Ensembl


ENSG00000115339


ENSMUSG00000026994

UniProt


Q14435


P70419

RefSeq (mRNA)


NM_004482


NM_015736

RefSeq (protein)


NP_004473


NP_056551

Location (UCSC)

Chr 2: 165.75 – 165.79 Mb

Chr 2: 66.08 – 66.12 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Polypeptide N-acetylgalactosaminyltransferase 3 is an enzyme that in humans is encoded by the GALNT3 gene.^[3]^[4]^[5]

This gene encodes UDP-GalNAc transferase 3, a member of the GalNAc-transferases 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.^[5]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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. PMID 9592121. doi:10.1093/glycob/8.6.547.
↑ 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. PMID 15133511. doi:10.1038/ng1358.
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. PMID 8663203. doi:10.1074/jbc.271.29.17006.
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. PMID 9295285. doi:10.1074/jbc.272.38.23503.
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. 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. PMID 9884405. doi:10.1093/glycob/9.1.43.
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. PMC 2364253 . PMID 12232759. doi:10.1038/sj.bjc.6600536.
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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
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. PMID 12506059. doi:10.1167/iovs.02-0181.
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. PMID 12708471. doi:10.1111/j.1349-7006.2003.tb01348.x.
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. PMID 14555840. doi:10.1159/000072957.
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. PMC 2409559 . PMID 14735190. doi:10.1038/sj.bjc.6601531.
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. PMID 15041730. doi:10.1158/1078-0432.CCR-1024-03.
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. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504.
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. PMID 15860931. doi:10.1159/000084117.
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. PMC 1356129 . PMID 16344560. doi:10.1101/gr.4039406.
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. PMID 16638743. doi:10.1074/jbc.M602469200.
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. PMID 16940445. doi:10.1210/jc.2006-1247.
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. PMID 17351710. doi:10.1007/s10038-007-0126-5.
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. PMID 17361208. doi:10.1038/modpathol.3800700.

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GALNT3

References

Further reading