Version 5.4
Mus musculus Protein: B3gnt1
Summary
InnateDB Protein IDBP-130614.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol B3gnt1
Protein Name UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1
Synonyms 1500032M01Rik; B3gnt6; BETA3GNT1; iGAT; iGNT;
Species Mus musculus
Ensembl Protein ENSMUSP00000062016
InnateDB Gene IDBG-130612 (B3gnt1)
Protein Structure
UniProt Annotation
Function Can initiate the synthesis or the elongation of the linear poly-N-acetyllactosaminoglycans. Involved in alpha- dystroglycan (DAG1) glycosylation (By similarity). {ECO:0000250}.
Subcellular Localization Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
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.
They are also associated with 4 interaction(s) predicted by orthology.
Predicted by orthology
Total 4 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0008532 N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity
Biological Process
GO:0006486 protein glycosylation
GO:0007411 axon guidance
GO:0030311 poly-N-acetyllactosamine biosynthetic process
Cellular Component
GO:0000139 Golgi membrane
GO:0016021 integral component of membrane
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID MGI:1919680
InterPro
PFAM
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8BWP8
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 108902
UniGene Mm.489654
RefSeq NP_780592
MGI ID
MGI Symbol B3gnt1
OMIM
CCDS CCDS29446
HPRD
IMGT
EMBL AK050347 AK083857 AK158899 BC002191 BC069927
GenPept AAH02191 AAH69927 BAC34203 BAC39041 BAE34720

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