ST6GALNAC4
From Wikipedia, the free encyclopedia
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ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4
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| Identifiers | ||||||||||||||
| Symbol(s) | ST6GALNAC4; SIAT3C; SIAT7D; ST6GALNACIV | |||||||||||||
| External IDs | OMIM: 606378 MGI: 1341894 HomoloGene: 7939 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| 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) |
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| 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:. 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:. 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:. 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:. 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:. PMID 17081983.

