GALNT1

GALNT1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases GALNT1, GALNAC-T1, polypeptide N-acetylgalactosaminyltransferase 1
External IDs MGI: 894693 HomoloGene: 8469 GeneCards: GALNT1
RNA expression pattern




More reference expression data
Orthologs
Species Human Mouse
Entrez

2589

14423

Ensembl

ENSG00000141429

ENSMUSG00000000420

UniProt

Q10472

O08912

RefSeq (mRNA)

NM_020474

NM_001160404
NM_013814

RefSeq (protein)

NP_065207.2

NP_001153876.1
NP_038842.3

Location (UCSC) Chr 18: 35.58 – 35.71 Mb Chr 18: 24.21 – 24.29 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Polypeptide N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the GALNT1 gene.[3][4][5]

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.[5]

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. ↑ 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.
  4. ↑ 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.
  5. 1 2 "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. 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. 
  • 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. 
  • "Toward a complete human genome sequence.". Genome Res. 8 (11): 1097–108. 1999. 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 139241Freely accessible. 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 528928Freely accessible. PMID 15489334. 


This article is issued from Wikipedia - version of the 5/31/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.