Identification |
HMDB Protein ID
| HMDBP09235 |
Secondary Accession Numbers
| |
Name
| UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8 |
Synonyms
|
- BGnT-8
- Beta-1,3-Gn-T8
- Beta-1,3-N-acetylglucosaminyltransferase 8
- Beta3Gn-T8
|
Gene Name
| B3GNT8 |
Protein Type
| Enzyme |
Biological Properties |
General Function
| Involved in galactosyltransferase activity |
Specific Function
| Beta-1,3-N-acetylglucosaminyltransferase that plays a role in the elongation of specific branch structures of multiantennary N-glycans. Has strong activity towards tetraantennary N-glycans and 2,6 triantennary glycans |
Pathways
|
Not Available
|
Reactions
| Not Available |
GO Classification
|
Component |
membrane |
cell part |
Function |
galactosyltransferase activity |
catalytic activity |
transferase activity |
transferase activity, transferring hexosyl groups |
transferase activity, transferring glycosyl groups |
Process |
metabolic process |
macromolecule metabolic process |
macromolecule modification |
protein modification process |
protein amino acid glycosylation |
|
Cellular Location
|
- Golgi apparatus membrane
- Single-pass type II membrane protein
|
Gene Properties |
Chromosome Location
| Chromosome:1 |
Locus
| 19q13.2 |
SNPs
| B3GNT8 |
Gene Sequence
|
>1194 bp
ATGCGCTGCCCCAAGTGCCTTCTCTGCCTGTCAGCACTGCTCACACTCCTGGGCCTCAAA
GTGTACATCGAGTGGACATCCGAGTCCCGGCTCAGCAAGGCCTACCCCAGCCCTCGGGGC
ACCCCGCCAAGCCCCACGCCAGCCAACCCTGAGCCCACCCTACCTGCCAACCTCTCCACC
CGCCTGGGCCAGACTATCCCGCTGCCCTTTGCTTACTGGAACCAGCAGCAGTGGCGGCTG
GGGTCCCTGCCCAGTGGGGACAGCACTGAAACGGGGGGCTGCCAGGCTTGGGGGGCCGCC
GCCGCCACCGAGATCCCTGACTTCGCCTCCTACCCCAAGGACCTCCGCCGCTTCTTGCTG
TCAGCAGCCTGCCGGAGCTTCCCACAGTGGCTGCCTGGAGGTGGTGGCAGCCAAGTCTCC
AGCTGCTCAGATACTGATGTCCCCTACCTGCTGTTGGCCGTCAAGTCAGAACCAGGGCGC
TTTGCAGAACGACAGGCCGTGAGAGAGACGTGGGGCAGTCCAGCTCCAGGGATCCGGCTG
CTCTTCCTGCTAGGGTCTCCGGTGGGTGAGGCGGGGCCTGACCTAGACTCACTAGTGGCC
TGGGAGAGCCGTCGCTACAGTGACCTGCTGCTCTGGGACTTCCTCGACGTCCCATTCAAC
CAGACGCTCAAAGACCTGCTGCTGCTGGCCTGGCTGGGCCGCCACTGCCCCACCGTGAGT
TTTGTCTTGCGAGCTCAGGACGATGCCTTTGTACACACCCCTGCCCTGCTGGCTCACCTG
CGGGCCCTGCCACCTGCCTCGGCCCGAAGCCTCTACCTGGGTGAGGTCTTTACCCAGGCC
ATGCCTCTCCGGAAGCCAGGAGGACCCTTCTATGTGCCCGAGTCCTTCTTCGAAGGTGGC
TACCCAGCCTATGCAAGCGGGGGTGGCTACGTCATTGCCGGGCGCCTGGCACCCTGGCTG
CTGCGGGCGGCAGCCCGTGTGGCACCCTTCCCCTTTGAGGACGTCTACACTGGCCTTTGC
ATCCGAGCCCTGGGCCTGGTGCCCCAGGCCCACCCAGGCTTCCTCACAGCCTGGCCAGCA
GACCGCACTGCGGACCACTGTGCTTTCCGCAACCTGCTGCTGGTACGGCCCCTGGGCCCC
CAGGCCAGCATTCGGCTCTGGAAACAACTGCAAGACCCAAGGCTCCAGTGCTGA
|
Protein Properties |
Number of Residues
| 397 |
Molecular Weight
| 43395.4 |
Theoretical pI
| 8.4 |
Pfam Domain Function
|
|
Signals
|
|
Transmembrane Regions
|
|
Protein Sequence
|
>UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8
MRCPKCLLCLSALLTLLGLKVYIEWTSESRLSKAYPSPRGTPPSPTPANPEPTLPANLST
RLGQTIPLPFAYWNQQQWRLGSLPSGDSTETGGCQAWGAAAATEIPDFASYPKDLRRFLL
SAACRSFPQWLPGGGGSQVSSCSDTDVPYLLLAVKSEPGRFAERQAVRETWGSPAPGIRL
LFLLGSPVGEAGPDLDSLVAWESRRYSDLLLWDFLDVPFNQTLKDLLLLAWLGRHCPTVS
FVLRAQDDAFVHTPALLAHLRALPPASARSLYLGEVFTQAMPLRKPGGPFYVPESFFEGG
YPAYASGGGYVIAGRLAPWLLRAAARVAPFPFEDVYTGLCIRALGLVPQAHPGFLTAWPA
DRTADHCAFRNLLLVRPLGPQASIRLWKQLQDPRLQC
|
External Links |
GenBank ID Protein
| 57207880 |
UniProtKB/Swiss-Prot ID
| Q7Z7M8 |
UniProtKB/Swiss-Prot Entry Name
| B3GN8_HUMAN |
PDB IDs
|
Not Available |
GenBank Gene ID
| AB175895 |
GeneCard ID
| B3GNT8 |
GenAtlas ID
| B3GNT8 |
HGNC ID
| HGNC:24139 |
References |
General References
| - Huang C, Zhou J, Wu S, Shan Y, Teng S, Yu L: Cloning and tissue distribution of the human B3GALT7 gene, a member of the beta1,3-Glycosyltransferase family. Glycoconj J. 2004;21(5):267-73. [PubMed:15486459 ]
- Ishida H, Togayachi A, Sakai T, Iwai T, Hiruma T, Sato T, Okubo R, Inaba N, Kudo T, Gotoh M, Shoda J, Tanaka N, Narimatsu H: A novel beta1,3-N-acetylglucosaminyltransferase (beta3Gn-T8), which synthesizes poly-N-acetyllactosamine, is dramatically upregulated in colon cancer. FEBS Lett. 2005 Jan 3;579(1):71-8. [PubMed:15620693 ]
- Seko A, Yamashita K: Characterization of a novel galactose beta1,3-N-acetylglucosaminyltransferase (beta3Gn-T8): the complex formation of beta3Gn-T2 and beta3Gn-T8 enhances enzymatic activity. Glycobiology. 2005 Oct;15(10):943-51. Epub 2005 May 25. [PubMed:15917431 ]
|