ST6GALNAC4

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ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4
Identifiers
Symbol(s) ST6GALNAC4; SIAT3C; SIAT7D; ST6GALNACIV
External IDs OMIM: 606378 MGI1341894 HomoloGene7939
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 27090 20448
Ensembl ENSG00000136840 n/a
Uniprot Q9H4F1 n/a
Refseq NM_175039 (mRNA)
NP_778204 (protein)
NM_011373 (mRNA)
NP_035503 (protein)
Location Chr 9: 129.71 - 129.72 Mb n/a
Pubmed search [1] [2]

ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4, also known as ST6GALNAC4, is a human gene.[1]

The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein prefers glycoproteins rather than glycolipids as substrates and shows restricted substrate specificity, utilizing only the trisaccharide sequence Neu5Ac-alpha-2,3-Gal-beta-1,3-GalNAc. In addition, it is involved in the synthesis of ganglioside GD1A from GM1B. The encoded protein is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. This protein is a member of glycosyltransferase family 29. Transcript variants encoding different isoforms have been found for this gene.[1]

[edit] References

[edit] Further reading

  • Lanfranchi G, Muraro T, Caldara F, et al. (1996). "Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization.". Genome Res. 6 (1): 35-42. PMID 8681137. 
  • Lee YC, Kaufmann M, Kitazume-Kawaguchi S, et al. (1999). "Molecular cloning and functional expression of two members of mouse NeuAcalpha2,3Galbeta1,3GalNAc GalNAcalpha2,6-sialyltransferase family, ST6GalNAc III and IV.". J. Biol. Chem. 274 (17): 11958-67. PMID 10207017. 
  • Gilley J, Fried M (1999). "Extensive gene order differences within regions of conserved synteny between the Fugu and human genomes: implications for chromosomal evolution and the cloning of disease genes.". Hum. Mol. Genet. 8 (7): 1313-20. PMID 10369878. 
  • Harduin-Lepers A, Stokes DC, Steelant WF, et al. (2001). "Cloning, expression and gene organization of a human Neu5Ac alpha 2-3Gal beta 1-3GalNAc alpha 2,6-sialyltransferase: hST6GalNAcIV.". Biochem. J. 352 Pt 1: 37-48. PMID 11062056. 
  • Moody AM, North SJ, Reinhold B, et al. (2003). "Sialic acid capping of CD8beta core 1-O-glycans controls thymocyte-major histocompatibility complex class I interaction.". J. Biol. Chem. 278 (9): 7240-6. doi:10.1074/jbc.M210468200. PMID 12459555. 
  • 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. PMID 12477932. 
  • Kim SW, Kang NY, Lee SH, et al. (2003). "Genomic structure and promoter analysis of human NeuAc alpha2,3Gal beta1,3GalNAc alpha2,6-sialyltransferase (hST6GalNAc IV) gene.". Gene 305 (1): 113-20. PMID 12594047. 
  • 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. PMID 15489334. 
  • Kang NY, Park YD, Choi HJ, et al. (2005). "Regulatory elements involved in transcription of the human NeuAcalpha2,3Galbeta1,3GalNAcalpha2,6-sialyltransferase (hST6GalNAc IV) gene.". Mol. Cells 18 (2): 157-62. PMID 15528990. 
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635-48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.