GALNT1

Polypeptide N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the GALNT1 gene.[5][6][7]

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)[1] Band 18q12.2 Start 35,581,117 bp[1] End 35,711,834 bp[1]
Gene location (Mouse) Chr. Chromosome 18 (mouse)[2] Band 18|18 A2 Start 24,205,344 bp[2] End 24,286,818 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity, transferring glycosyl groups • 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: 24.21 – 24.29 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000141429 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000000420 - 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.
5. White T, Bennett EP, Takio K, Sorensen T, Bonding N, Clausen H (Dec 1995). "Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase". J Biol Chem. 270 (41): 24156–65. doi:10.1074/jbc.270.41.24156. PMID 7592619.
6. Tenno M, Toba S, Kezdy FJ, Elhammer AP, Kurosaka A (Aug 2002). "Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)". Eur J Biochem. 269 (17): 4308–16. doi:10.1046/j.1432-1033.2002.03123.x. PMID 12199709.
7. "Entrez Gene: GALNT1 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)".

Further reading

• Paulson JC, Colley KJ (1989). "Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation". J. Biol. Chem. 264 (30): 17615–8. 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. 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. 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. 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.