Version 5.4
Mus musculus Protein: B3gnt8
Summary
InnateDB Protein IDBP-158030.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol B3gnt8
Protein Name UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000092277
InnateDB Gene IDBG-158028 (B3gnt8)
Protein Structure
UniProt Annotation
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 (By similarity). {ECO:0000250UniProtKB:Q7Z7M8}.
Subcellular Localization Golgi apparatus membrane {ECO:0000250UniProtKB:Q9NY97}; Single-pass type II membrane protein {ECO:0000250UniProtKB:Q9NY97}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0008378 galactosyltransferase activity
GO:0016262 protein N-acetylglucosaminyltransferase activity
Biological Process
GO:0006486 protein glycosylation
GO:0030311 poly-N-acetyllactosamine biosynthetic process
Cellular Component
GO:0000139 Golgi membrane
GO:0005575 cellular_component
GO:0016020 membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:2385269
InterPro IPR002659 Glycosyl transferase, family 31
PFAM PF01762
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8R3I9
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 232984
UniGene Mm.192369
RefSeq NP_666296
MGI ID
MGI Symbol B3gnt8
OMIM
CCDS CCDS20989
HPRD
IMGT
EMBL AK042388 AK154220 AK154901 BC025206
GenPept AAH25206 BAC31246 BAE32443 BAE32912

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca