Version 5.4
Mus musculus Protein: B3galtl
Summary
InnateDB Protein IDBP-209471.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol B3galtl
Protein Name beta 1,3-galactosyltransferase-like
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000097972
InnateDB Gene IDBG-209467 (B3galtl)
Protein Structure
UniProt Annotation
Function O-fucosyltransferase that transfers glucose toward fucose with a beta-1,3 linkage. Specifically glucosylates O-linked fucosylglycan on TSP type-1 domains of proteins, thereby contributing to elongation of O-fucosylglycan (By similarity). {ECO:0000250}.
Subcellular Localization Endoplasmic reticulum membrane {ECO:0000255PROSITE-ProRule:PRU10138}; 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.
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0016757 transferase activity, transferring glycosyl groups
Biological Process
GO:0006004 fucose metabolic process
GO:0006486 protein glycosylation
GO:0008150 biological_process
Cellular Component
GO:0005575 cellular_component
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:2685903
InterPro IPR003378 Fringe-like
IPR029044 Nucleotide-diphospho-sugar transferases
PFAM PF02434
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8BHT6
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 381694
UniGene Mm.45060
RefSeq NP_001074673
MGI ID
MGI Symbol B3glct
OMIM
CCDS CCDS39410
HPRD
IMGT
EMBL AB253762 AC114342 AK089440 BC115781 BC117522
GenPept AAI15782 AAI17523 BAC40885 BAF02833

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