Protein-coding gene in the species Homo sapiens
ST6GALNAC4 |
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Identifiers |
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Aliases | ST6GALNAC4, IV, SIAT3-C, SIAT3C, SIAT7-D, SIAT7D, ST6GALNACIV, ST6GalNAc, ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 4 |
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External IDs | OMIM: 606378; MGI: 1341894; HomoloGene: 7939; GeneCards: ST6GALNAC4; OMA:ST6GALNAC4 - orthologs |
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Gene location (Human) |
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| Chr. | Chromosome 9 (human)[1] |
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| Band | 9q34.11 | Start | 127,907,886 bp[1] |
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End | 127,917,041 bp[1] |
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Gene location (Mouse) |
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| Chr. | Chromosome 2 (mouse)[2] |
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| Band | 2|2 B | Start | 32,477,107 bp[2] |
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End | 32,489,710 bp[2] |
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RNA expression pattern |
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Bgee | Human | Mouse (ortholog) |
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Top expressed in | - body of pancreas
- apex of heart
- upper lobe of left lung
- spleen
- right auricle
- right ovary
- right coronary artery
- mucosa of transverse colon
- left ventricle
- left coronary artery
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| Top expressed in | - cerebellar cortex
- dentate gyrus of hippocampal formation granule cell
- granulocyte
- muscle of thigh
- superior frontal gyrus
- primary visual cortex
- stroma of bone marrow
- embryo
- left colon
- lumbar subsegment of spinal cord
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| More reference expression data |
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BioGPS |
| More reference expression data |
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Gene ontology |
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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 |
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Orthologs |
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Species | Human | Mouse |
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Entrez | | |
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Ensembl | | |
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UniProt | | |
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RefSeq (mRNA) | |
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NM_014403 NM_175039 NM_175040 |
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RefSeq (protein) | | |
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Location (UCSC) | Chr 9: 127.91 – 127.92 Mb | Chr 2: 32.48 – 32.49 Mb |
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PubMed search | [3] | [4] |
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Wikidata |
View/Edit Human | View/Edit Mouse |
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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.[5]
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.[5]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000136840 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000079442 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b "Entrez Gene: ST6GALNAC4 ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4".
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.
- 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.