GALNT1

GALNT1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1XHB
Identifiers
Aliases	GALNT1, GALNAC-T1, polypeptide N-acetylgalactosaminyltransferase 1
External IDs	OMIM: 602273 MGI: 894693 HomoloGene: 8469 GeneCards: GALNT1
Gene location (Human) Chr. Chromosome 18 (human) Band 18q12.2 Start 35,581,117 bp End 35,711,834 bp
Gene location (Mouse) Chr. Chromosome 18 (mouse) Band 18|18 A2 Start 24,338,401 bp End 24,419,875 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in nipple amniotic fluid oral cavity tibia superior surface of tongue lactiferous duct retinal pigment epithelium periodontal fiber jejunal mucosa body of tongue Top expressed in molar blood proximal tubule parotid gland fossa ciliary body cumulus cell Paneth cell membranous bone condyle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function glycosyltransferase activity polypeptide N-acetylgalactosaminyltransferase activity transferase activity manganese ion binding metal ion binding carbohydrate binding Cellular component perinuclear region of cytoplasm integral component of membrane extracellular region Golgi cisterna membrane Golgi membrane Golgi apparatus membrane endoplasmic reticulum membrane Biological process protein glycosylation protein O-linked glycosylation via serine protein O-linked glycosylation via threonine O-glycan processing protein O-linked glycosylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2589 14423 Ensembl ENSG00000141429 ENSMUSG00000000420 UniProt Q10472 O08912 RefSeq (mRNA) NM_020474 NM_001160404 NM_013814 NM_001361200 RefSeq (protein) NP_065207 NP_001153876 NP_038842 NP_001348129 Location (UCSC) Chr 18: 35.58 – 35.71 Mb Chr 18: 24.34 – 24.42 Mb PubMed search
Wikidata
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Polypeptide N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the GALNT1 gene.

This gene encodes a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc transferase motif, and a C-terminal ricin/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression. Transcript variants derived from this gene that utilize alternative polyA signals have been described in the literature.

Further reading

• Paulson JC, Colley KJ (1989). "Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation". J. Biol. Chem. 264 (30): 17615–8. doi:10.1016/S0021-9258(19)84610-0. PMID 2681181.
• 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.
• Meurer JA, Naylor JM, Baker CA, et al. (1996). "cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase". J. Biochem. 118 (3): 568–74. doi:10.1093/oxfordjournals.jbchem.a124947. PMID 8690719.
• Meurer JA, Drong RF, Homa FL, et al. (1996). "Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene". Glycobiology. 6 (2): 231–41. doi:10.1093/glycob/6.2.231. PMID 8727794.
• Takai S, Hinoda Y, Adachi T, et al. (1997). "A human UDP-GalNAc: polypeptide, N-acetylgalactosaminyltransferase type 1 gene is located at the chromosomal region 18q12.1". Hum. Genet. 99 (3): 293–4. doi:10.1007/s004390050359. PMID 9050910. S2CID 22965327.
• 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.
• Müller S, Goletz S, Packer N, et al. (1997). "Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo". J. Biol. Chem. 272 (40): 24780–93. doi:10.1074/jbc.272.40.24780. PMID 9312074.
• 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.
• Bennett EP, Weghuis DO, Merkx G, et al. (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.
• Sanger Centre, The; Washington University Genome Sequencing Cente, The (1999). "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. doi:10.1101/gr.8.11.1097. PMID 9847074.
• Tenno M, Saeki A, Kézdy FJ, et al. (2003). "The lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites". J. Biol. Chem. 277 (49): 47088–96. doi:10.1074/jbc.M207369200. PMID 12364335.
• 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.
• Kinarsky L, Suryanarayanan G, Prakash O, et al. (2004). "Conformational studies on the MUC1 tandem repeat glycopeptides: implication for the enzymatic O-glycosylation of the mucin protein core". Glycobiology. 13 (12): 929–39. doi:10.1093/glycob/cwg109. PMID 12925576.
• Brokx RD, Revers L, Zhang Q, et al. (2004). "Nuclear magnetic resonance-based dissection of a glycosyltransferase specificity for the mucin MUC1 tandem repeat". Biochemistry. 42 (47): 13817–25. CiteSeerX 10.1.1.879.1929. doi:10.1021/bi0353070. PMID 14636048.
• 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.