Version 5.4
Mus musculus Protein: A3galt2
Summary
InnateDB Protein IDBP-269522.5
Last Modified 2012-02-14 [Report errors or provide feedback]
Gene Symbol A3galt2
Protein Name alpha 1,3-galactosyltransferase 2 (isoglobotriaosylceramide synthase)
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000101687
InnateDB Gene IDBG-190157 (A3galt2)
Protein Structure
UniProt Annotation
Function
Subcellular Localization
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:0001962 alpha-1,3-galactosyltransferase activity
GO:0016758 transferase activity, transferring hexosyl groups
GO:0046872 metal ion binding
GO:0047276 N-acetyllactosaminide 3-alpha-galactosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006486 protein glycosylation
GO:0006688 glycosphingolipid biosynthetic process
GO:0030259 lipid glycosylation
Cellular Component
GO:0005794 Golgi apparatus
GO:0016020 membrane
GO:0016021 integral component of membrane
GO:0031982 vesicle
GO:0032580 Golgi cisterna membrane
Protein Structure and Domains
PDB ID MGI:2685279
InterPro IPR005076 Glycosyl transferase, family 6
IPR029044 Nucleotide-diphospho-sugar transferases
PFAM PF03414
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q3V1N9
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 215493
UniGene Mm.300900
RefSeq XP_006502987
MGI ID
MGI Symbol A3galt2
OMIM
CCDS
HPRD
IMGT
EMBL AK132334 AL611983 AY491982 CU467499
GenPept AAS66769 BAE21111 CAQ52295 CAQ52296

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