Version 5.4
Mus musculus Protein: Alg3
Summary
InnateDB Protein IDBP-145123.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Alg3
Protein Name asparagine-linked glycosylation 3 homolog (yeast, alpha-1,3-mannosyltransferase)
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000045272
InnateDB Gene IDBG-145121 (Alg3)
Protein Structure
UniProt Annotation
Function Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc2-PP-Dol.
Subcellular Localization Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
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 1 interaction(s) predicted by orthology.
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000033 alpha-1,3-mannosyltransferase activity
GO:0016758 transferase activity, transferring hexosyl groups
GO:0052925 dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity
Biological Process
GO:0006486 protein glycosylation
GO:0097502 mannosylation
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1098592
InterPro IPR007873 Glycosyltransferase, ALG3
PFAM PF05208
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8K2A8
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 208624
UniGene Mm.467469
RefSeq NP_666051
MGI ID
MGI Symbol Alg3
OMIM
CCDS CCDS37289
HPRD
IMGT
EMBL AC087898 BC031893
GenPept AAH31893

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