ST6GALNAC4

ST6GALNAC4
Identifiers
Aliases	ST6GALNAC4, IV, SIAT3-C, SIAT3C, SIAT7-D, SIAT7D, ST6GALNACIV, ST6GalNAc, ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 4
External IDs	OMIM: 606378 MGI: 1341894 HomoloGene: 7939 GeneCards: ST6GALNAC4
Gene location (Human) Chr. Chromosome 9 (human) Band 9q34.11 Start 127,907,886 bp End 127,917,041 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 B Start 32,477,107 bp End 32,489,710 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas upper lobe of left lung spleen right coronary artery left ventricle left coronary artery blood trabecular bone bone marrow stromal cell of endometrium Top expressed in cerebellar cortex superior frontal gyrus left colon body of femur temporal muscle vastus lateralis muscle endocardial cushion soleus muscle neural tube ascending aorta More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity glycosyltransferase activity sialyltransferase activity (alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetyl-galactosaminide 6-alpha-sialyltransferase activity alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity Cellular component integral component of membrane Golgi apparatus membrane Golgi membrane Biological process O-glycan processing protein glycosylation oligosaccharide metabolic process glycolipid metabolic process sialylation protein N-linked glycosylation via asparagine Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 27090 20448 Ensembl ENSG00000136840 ENSMUSG00000079442 UniProt Q9H4F1 Q9R2B6 RefSeq (mRNA) NM_014403 NM_175039 NM_175040 NM_001276425 NM_011373 RefSeq (protein) NP_778204 NP_778205 NP_001263354 NP_035503 Location (UCSC) Chr 9: 127.91 – 127.92 Mb Chr 2: 32.48 – 32.49 Mb PubMed search
Wikidata
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ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4, also known as sialyltransferase 3C (SIAT3-C) or sialyltransferase 7D (SIAT7-D) is a sialyltransferase enzyme that in humans is encoded by the ST6GALNAC4 gene.

Function

ST6GALNAC4 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 enzyme 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.

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. doi:10.1101/gr.6.1.35. 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. doi:10.1074/jbc.274.17.11958. 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. doi:10.1093/hmg/8.7.1313. 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 (Pt 1): 37–48. PMC 1221430. 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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. doi:10.1016/S0378-1119(02)01234-9. 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. PMC 528928. 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. doi:10.1016/S1016-8478(23)13096-2. 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. S2CID 7827573.