GALNT6

Protein-coding gene in humans
GALNT6
Identifiers
AliasesGALNT6, GALNAC-T6, GalNAcT6, polypeptide N-acetylgalactosaminyltransferase 6
External IDsOMIM: 605148; MGI: 1891640; HomoloGene: 5218; GeneCards: GALNT6; OMA:GALNT6 - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for GALNT6
Genomic location for GALNT6
Band12q13.13Start51,351,247 bp[1]
End51,392,867 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • parotid gland

  • trachea

  • corpus epididymis

  • bronchial epithelial cell

  • pylorus

  • jejunal mucosa

  • duodenum

  • stromal cell of endometrium

  • monocyte

  • corpus callosum
    n/a
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • carbohydrate binding
  • glycosyltransferase activity
  • metal ion binding
  • transferase activity
  • polypeptide N-acetylgalactosaminyltransferase activity
Cellular component
  • membrane
  • perinuclear region of cytoplasm
  • Golgi membrane
  • integral component of membrane
  • Golgi apparatus
Biological process
  • O-glycan processing
  • protein O-linked glycosylation
  • protein glycosylation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

11226

207839

Ensembl

ENSG00000139629

n/a

UniProt

Q8NCL4

Q8C7U7

RefSeq (mRNA)

NM_007210

NM_001161767
NM_001161768
NM_172451

RefSeq (protein)

NP_009141

NP_001155239
NP_001155240
NP_766039

Location (UCSC)Chr 12: 51.35 – 51.39 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Polypeptide N-acetylgalactosaminyltransferase 6 is an enzyme that in humans is encoded by the GALNT6 gene.[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. The encoded protein is capable of glycosylating fibronectin peptide in vitro and is expressed in a fibroblast cell line, indicating that it may be involved in the synthesis of oncofetal fibronectin.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000139629 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Bennett EP, Hassan H, Mandel U, Hollingsworth MA, Akisawa N, Ikematsu Y, Merkx G, van Kessel AG, Olofsson S, Clausen H (Oct 1999). "Cloning and characterization of a close homologue of human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy". J Biol Chem. 274 (36): 25362–70. doi:10.1074/jbc.274.36.25362. hdl:2066/184726. PMID 10464263.
  5. ^ a b "Entrez Gene: GALNT6 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 6 (GalNAc-T6)".

Further reading

  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • 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.
  • 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. doi:10.1167/iovs.02-0181. PMID 12506059.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • 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.
  • Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.
  • 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. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.


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