Biology:GALNT1

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Short description: Protein-coding gene in the species Homo sapiens

A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Polypeptide N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the GALNT1 gene.[1][2][3]

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.[3]

References

  1. ↑ "Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase". The Journal of Biological Chemistry 270 (41): 24156–24165. December 1995. doi:10.1074/jbc.270.41.24156. PMID 7592619. 
  2. ↑ "Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)". European Journal of Biochemistry 269 (17): 4308–4316. August 2002. doi:10.1046/j.1432-1033.2002.03123.x. PMID 12199709. 
  3. ↑ 3.0 3.1 "Entrez Gene: GALNT1 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=2589. 

Further reading

  • "Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation.". The Journal of Biological Chemistry 264 (30): 17615–17618. 1989. doi:10.1016/S0021-9258(19)84610-0. PMID 2681181. 
  • "cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.". The Journal of Biological Chemistry 271 (29): 17006–17012. 1996. doi:10.1074/jbc.271.29.17006. PMID 8663203. 
  • "cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase". Journal of Biochemistry 118 (3): 568–574. September 1995. doi:10.1093/oxfordjournals.jbchem.a124947. PMID 8690719. 
  • "Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene". Glycobiology 6 (2): 231–241. March 1996. doi:10.1093/glycob/6.2.231. PMID 8727794. 
  • "A human UDP-GalNAc: polypeptide, N-acetylgalactosaminyltransferase type 1 gene is located at the chromosomal region 18q12.1". Human Genetics 99 (3): 293–294. March 1997. doi:10.1007/s004390050359. PMID 9050910. 
  • "Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3". The Journal of Biological Chemistry 272 (38): 23503–23514. September 1997. doi:10.1074/jbc.272.38.23503. PMID 9295285. 
  • "Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo". The Journal of Biological Chemistry 272 (40): 24780–24793. October 1997. doi:10.1074/jbc.272.40.24780. PMID 9312074. 
  • "Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus". Journal of Cell Science 111 ( Pt 1) (1): 45–60. January 1998. doi:10.1242/jcs.111.1.45. PMID 9394011. 
  • "Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family". Glycobiology 8 (6): 547–555. June 1998. doi:10.1093/glycob/8.6.547. PMID 9592121. 
  • "Toward a complete human genome sequence". Genome Research 8 (11): 1097–1108. November 1998. doi:10.1101/gr.8.11.1097. PMID 9847074. 
  • "The lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites". The Journal of Biological Chemistry 277 (49): 47088–47096. December 2002. doi:10.1074/jbc.M207369200. PMID 12364335. 
  • "Conformational studies on the MUC1 tandem repeat glycopeptides: implication for the enzymatic O-glycosylation of the mucin protein core". Glycobiology 13 (12): 929–939. December 2003. doi:10.1093/glycob/cwg109. PMID 12925576. 
  • "Nuclear magnetic resonance-based dissection of a glycosyltransferase specificity for the mucin MUC1 tandem repeat". Biochemistry 42 (47): 13817–13825. December 2003. doi:10.1021/bi0353070. PMID 14636048. 



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