B4GALNT1

Beta-1,4-N-acetyl-galactosaminyl transferase 1
Identifiers
Symbols	B4GALNT1 ; GALGT; GALNACT; GalNAc-T; SPG26
External IDs	OMIM: 601873 MGI: 1342057 HomoloGene: 1133 GeneCards: B4GALNT1 Gene
EC number	2.4.1.92
Gene ontology Molecular function • (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase activity Cellular component • plasma membrane • membrane • integral component of Golgi membrane Biological process • ganglioside biosynthetic process • carbohydrate metabolic process • protein glycosylation • glycosphingolipid metabolic process • spermatogenesis • lipid storage • lipid glycosylation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2583	14421
Ensembl	ENSG00000135454	ENSMUSG00000006731
UniProt	Q00973	Q09200
RefSeq (mRNA)	NM_001276468	NM_001244617
RefSeq (protein)	NP_001263397	NP_001231546
Location (UCSC)	Chr 12: 57.62 – 57.63 Mb	Chr 10: 127.17 – 127.17 Mb
PubMed search

Beta-1,4 N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the B4GALNT1 gene.^[1][2]

GM2 and GD2 gangliosides are sialic acid-containing glycosphingolipids. GalNAc-T is the enzyme involved in the biosynthesis of G(M2) and G(D2) glycosphingolipids. GalNAc-T catalyzes the transfer of GalNAc into G(M3) and G(D3) by a beta-1,4 linkage, resulting in the synthesis of G(M2) and G(D2), respectively.^[2]

References

1. Nagata Y, Yamashiro S, Yodoi J, Lloyd KO, Shiku H, Furukawa K (Jul 1992). "Expression cloning of beta 1,4 N-acetylgalactosaminyltransferase cDNAs that determine the expression of GM2 and GD2 gangliosides". J Biol Chem 267 (17): 12082–9. PMID 1601877.
2. "Entrez Gene: B4GALNT1 beta-1,4-N-acetyl-galactosaminyl transferase 1".

Further reading

• Nagata Y, Yamashiro S, Yodoi J; et al. (1994). "Expression cloning of beta 1,4 N-acetylgalactosaminyltransferase cDNAs that determine the expression of GM2 and GD2 gangliosides.". J. Biol. Chem. 269 (9): 7045. PMID 8120069.
• Meurer JA, Naylor JM, Baker CA; et al. (1996). "cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase.". J. Biochem. 118 (3): 568–74. PMID 8690719.
• Furukawa K, Soejima H, Niikawa N, Shiku H (1996). "Genomic organization and chromosomal assignment of the human beta1, 4-N-acetylgalactosaminyltransferase gene. Identification of multiple transcription units.". J. Biol. Chem. 271 (34): 20836–44. doi:10.1074/jbc.271.34.20836. PMID 8702839.
• Jaskiewicz E, Zhu G, Bassi R; et al. (1996). "Beta1,4-N-acetylgalactosaminyltransferase (GM2 synthase) is released from Golgi membranes as a neuraminidase-sensitive, disulfide-bonded dimer by a cathepsin D-like protease.". J. Biol. Chem. 271 (42): 26395–403. doi:10.1074/jbc.271.42.26395. PMID 8824296.
• Giraudo CG, Rosales Fritz VM, Maccioni HJ (1999). "GA2/GM2/GD2 synthase localizes to the trans-golgi network of CHO-K1 cells.". Biochem. J. 342 Pt 3: 633–40. PMC 1220504. PMID 10477274.
• Toba S, Tenno M, Konishi M; et al. (2000). "Brain-specific expression of a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T9).". Biochim. Biophys. Acta 1493 (1-2): 264–8. doi:10.1016/S0167-4781(00)00180-9. PMID 10978536.
• Li J, Yen TY, Allende ML; et al. (2001). "Disulfide bonds of GM2 synthase homodimers. Antiparallel orientation of the catalytic domains.". J. Biol. Chem. 275 (52): 41476–86. doi:10.1074/jbc.M007480200. PMID 11018043.
• 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.
• Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Gornati R, Chini V, Rimoldi S; et al. (2007). "Evaluation of SAT-1, SAT-2 and GalNAcT-1 mRNA in colon cancer by real-time PCR.". Mol. Cell. Biochem. 298 (1-2): 59–68. doi:10.1007/s11010-006-9350-0. PMID 17119850.