Version 5.4
Homo sapiens Protein: ALG2
Summary
InnateDB Protein IDBP-596883.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol ALG2
Protein Name asparagine-linked glycosylation 2, alpha-1,3-mannosyltransferase homolog (S. cerevisiae)
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000432675
InnateDB Gene IDBG-78514 (ALG2)
Protein Structure
UniProt Annotation
Function Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)- dolichol diphosphate. {ECO:0000269PubMed:12684507}.
Subcellular Localization Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Disease Associations Congenital disorder of glycosylation 1I (CDG1I) [MIM:607906]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269PubMed:12684507}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 23 experimentally validated interaction(s) in this database.
Experimentally validated
Total 23 [view]
Protein-Protein 22 [view]
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Protein Structure and Domains
PDB ID
InterPro
PFAM
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-Q9H553
TrEMBL
UniProt Splice Variant
Entrez Gene 85365
UniGene Hs.40919
RefSeq
HUGO HGNC:23159
OMIM 607905
CCDS
HPRD 09716
IMGT
EMBL
GenPept

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