Version 5.4
Mus musculus Protein: Alg11
Summary
InnateDB Protein IDBP-259634.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Alg11
Protein Name asparagine-linked glycosylation 11 homolog (yeast, alpha-1,2-mannosyltransferase)
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000106365
InnateDB Gene IDBG-139624 (Alg11)
Protein Structure
UniProt Annotation
Function Mannosyltransferase involved in the last steps of the synthesis of Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum. Catalyzes the addition of the 4th and 5th mannose residues to the dolichol- linked oligosaccharide chain (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 2 experimentally validated interaction(s) in this database.
They are also associated with 2 interaction(s) predicted by orthology.
Experimentally validated
Total 2 [view]
Protein-Protein 2 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 2 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0004377 GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity
Biological Process
GO:0009058 biosynthetic process
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:2142632
InterPro IPR001296 Glycosyl transferase, family 1
PFAM PF00534
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q3TZM9
PhosphoSite PhosphoSite-Q3TZM9
TrEMBL
UniProt Splice Variant
Entrez Gene 207958
UniGene Mm.489240
RefSeq NP_898965
MGI ID
MGI Symbol Alg11
OMIM
CCDS CCDS40292
HPRD
IMGT
EMBL AK046475 AK157746 BC061469
GenPept AAH61469 BAC32746 BAE34179

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