B4GALNT1

Beta-1,4-N-acetyl-galactosaminyl transferase 1, also known as B4GALNT1, is a human gene.cite web | title = Entrez Gene: B4GALNT1 beta-1,4-N-acetyl-galactosaminyl transferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2583| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: B4GALNT1 beta-1,4-N-acetyl-galactosaminyl transferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2583| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Nagata Y, Yamashiro S, Yodoi J, "et al." |title=Expression cloning of beta 1,4 N-acetylgalactosaminyltransferase cDNAs that determine the expression of GM2 and GD2 gangliosides. |journal=J. Biol. Chem. |volume=267 |issue= 17 |pages= 12082–9 |year= 1992 |pmid= 1601877 |doi=
*cite journal | author=Nagata Y, Yamashiro S, Yodoi J, "et al." |title=Expression cloning of beta 1,4 N-acetylgalactosaminyltransferase cDNAs that determine the expression of GM2 and GD2 gangliosides. |journal=J. Biol. Chem. |volume=269 |issue= 9 |pages= 7045 |year= 1994 |pmid= 8120069 |doi=
*cite journal | author=Meurer JA, Naylor JM, Baker CA, "et al." |title=cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase. |journal=J. Biochem. |volume=118 |issue= 3 |pages= 568–74 |year= 1996 |pmid= 8690719 |doi=
*cite journal | author=Furukawa K, Soejima H, Niikawa N, Shiku H |title=Genomic organization and chromosomal assignment of the human beta1, 4-N-acetylgalactosaminyltransferase gene. Identification of multiple transcription units. |journal=J. Biol. Chem. |volume=271 |issue= 34 |pages= 20836–44 |year= 1996 |pmid= 8702839 |doi=
*cite journal | author=Jaskiewicz E, Zhu G, Bassi R, "et al." |title=Beta1,4-N-acetylgalactosaminyltransferase (GM2 synthase) is released from Golgi membranes as a neuraminidase-sensitive, disulfide-bonded dimer by a cathepsin D-like protease. |journal=J. Biol. Chem. |volume=271 |issue= 42 |pages= 26395–403 |year= 1996 |pmid= 8824296 |doi=
*cite journal | author=Giraudo CG, Rosales Fritz VM, Maccioni HJ |title=GA2/GM2/GD2 synthase localizes to the trans-golgi network of CHO-K1 cells. |journal=Biochem. J. |volume=342 Pt 3 |issue= |pages= 633–40 |year= 1999 |pmid= 10477274 |doi=
*cite journal | author=Toba S, Tenno M, Konishi M, "et al." |title=Brain-specific expression of a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T9). |journal=Biochim. Biophys. Acta |volume=1493 |issue= 1-2 |pages= 264–8 |year= 2000 |pmid= 10978536 |doi=
*cite journal | author=Li J, Yen TY, Allende ML, "et al." |title=Disulfide bonds of GM2 synthase homodimers. Antiparallel orientation of the catalytic domains. |journal=J. Biol. Chem. |volume=275 |issue= 52 |pages= 41476–86 |year= 2001 |pmid= 11018043 |doi= 10.1074/jbc.M007480200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209
*cite journal | author=Gornati R, Chini V, Rimoldi S, "et al." |title=Evaluation of SAT-1, SAT-2 and GalNAcT-1 mRNA in colon cancer by real-time PCR. |journal=Mol. Cell. Biochem. |volume=298 |issue= 1-2 |pages= 59–68 |year= 2007 |pmid= 17119850 |doi= 10.1007/s11010-006-9350-0

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