Version 5.4
Mus musculus Protein: Alg8
Summary
InnateDB Protein IDBP-199646.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Alg8
Protein Name asparagine-linked glycosylation 8 homolog (yeast, alpha-1,3-glucosyltransferase)
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000095901
InnateDB Gene IDBG-199642 (Alg8)
Protein Structure
UniProt Annotation
Function Adds the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol (By similarity). {ECO:0000250}.
Subcellular Localization Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass 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 3 interaction(s) predicted by orthology.
Predicted by orthology
Total 3 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000033 alpha-1,3-mannosyltransferase activity
GO:0016758 transferase activity, transferring hexosyl groups
Biological Process
GO:0006487 protein N-linked glycosylation
GO:0097502 mannosylation
Cellular Component
GO:0005575 cellular_component
GO:0005789 endoplasmic reticulum membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:2141959
InterPro IPR004856 Glycosyl transferase, ALG6/ALG8
PFAM PF03155
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q6P8H8
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 381903
UniGene Mm.418645
RefSeq NP_950200
MGI ID
MGI Symbol Alg8
OMIM
CCDS CCDS52313
HPRD
IMGT
EMBL AC155933 AK166755 AK166897 BC061244 CH466531
GenPept AAH61244 BAE38996 BAE39100 EDL16291

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