B4GALNT1

Beta-1,4 N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the B4GALNT1 gene.[5][6]

B4GALNT1
Identifiers
Aliases	B4GALNT1, GALGT, GALNACT, GalNAc-T, SPG26, beta-1,4-N-acetyl-galactosaminyltransferase 1
External IDs	OMIM: 601873 MGI: 1342057 HomoloGene: 1133 GeneCards: B4GALNT1
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q13.3 Start 57,623,409 bp[1] End 57,633,239 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10 D3|10 74.5 cM Start 127,165,225 bp[2] End 127,172,330 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity, transferring hexosyl groups • transferase activity, transferring glycosyl groups • acetylgalactosaminyltransferase activity • transferase activity • (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase activity Cellular component • Golgi apparatus • cell membrane • membrane • integral component of Golgi membrane • integral component of membrane • Golgi membrane Biological process • glycosphingolipid metabolic process • spermatogenesis • lipid glycosylation • lipid storage • ganglioside biosynthetic process • lipid metabolism • sphingolipid metabolic process • carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2583	14421
Ensembl	ENSG00000135454	ENSMUSG00000006731
UniProt	Q00973	Q09200
RefSeq (mRNA)	NM_001276468 NM_001276469 NM_001478	NM_001244617 NM_001244618 NM_008080 NM_027739 NM_001358577 NM_001358578
RefSeq (protein)	NP_001263397 NP_001263398 NP_001469	NP_001231546 NP_001231547 NP_032106 NP_082015 NP_001345506 NP_001345507
Location (UCSC)	Chr 12: 57.62 – 57.63 Mb	Chr 10: 127.17 – 127.17 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000135454 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000006731 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: B4GALNT1 beta-1,4-N-acetyl-galactosaminyl transferase 1".

External links

• Human B4GALNT1 genome location and B4GALNT1 gene details page in the UCSC Genome Browser.

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. doi:10.1093/oxfordjournals.jbchem.a124947. 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 (3): 633–40. doi:10.1042/bj3420633. 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• 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. S2CID 29889795.