ST6GALNAC2

Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 is an enzyme that in humans is encoded by the ST6GALNAC2 gene.[4][5]

ST6GALNAC2
Identifiers
Aliases	ST6GALNAC2, SAITL1, SIAT7, SIAT7B, SIATL1, ST6GalNAII, STHM, ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 2
External IDs	OMIM: 610137 MGI: 107553 HomoloGene: 4714 GeneCards: ST6GALNAC2
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17q25.1 Start 76,565,377 bp[1] End 76,586,956 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity, transferring glycosyl groups • transferase activity • sialyltransferase activity • alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity Cellular component • integral component of membrane • Golgi apparatus • membrane • Golgi membrane Biological process • sialylation • oligosaccharide metabolic process • O-glycan processing • protein N-linked glycosylation via asparagine • protein glycosylation • protein O-linked glycosylation • protein sialylation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10610	20446
Ensembl	ENSG00000070731	ENSMUSG00000057286
UniProt	Q9UJ37	P70277
RefSeq (mRNA)	NM_006456	NM_009180
RefSeq (protein)	NP_006447	NP_033206
Location (UCSC)	Chr 17: 76.57 – 76.59 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

References

1. GRCh38: Ensembl release 89: ENSG00000070731 - 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. Sotiropoulou G, Kono M, Anisowicz A, Stenman G, Tsuji S, Sager R (May 2002). "Identification and functional characterization of a human GalNAc [alpha]2,6-sialyltransferase with altered expression in breast cancer". Mol Med. 8 (1): 42–55. doi:10.1007/BF03402002. PMC 2039932. PMID 11984005.
5. "Entrez Gene: ST6GALNAC2 ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2".

Further reading

• Li GS, Zhu L, Zhang H, et al. (2007). "Variants of the ST6GALNAC2 promoter influence transcriptional activity and contribute to genetic susceptibility to IgA nephropathy". Hum. Mutat. 28 (10): 950–7. doi:10.1002/humu.20543. PMID 17480010. S2CID 7286057.
• Raska M, Moldoveanu Z, Suzuki H, et al. (2007). "Identification and characterization of CMP-NeuAc:GalNAc-IgA1 alpha2,6-sialyltransferase in IgA1-producing cells". J. Mol. Biol. 369 (1): 69–78. doi:10.1016/j.jmb.2007.03.002. PMC 1995659. PMID 17418236.
• 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.
• Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• 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. PMC 139241. PMID 12477932.
• Samyn-Petit B, Krzewinski-Recchi MA, Steelant WF, et al. (2000). "Molecular cloning and functional expression of human ST6GalNAc II. Molecular expression in various human cultured cells". Biochim. Biophys. Acta. 1474 (2): 201–11. doi:10.1016/s0304-4165(00)00020-9. PMID 10742600.
• 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.
• 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.