Version 5.4
Mus musculus Protein: Ost4
Summary
InnateDB Protein IDBP-625630.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ost4
Protein Name oligosaccharyltransferase 4 homolog (S. cerevisiae)
Synonyms 2310016E02Rik;
Species Mus musculus
Ensembl Protein ENSMUSP00000128352
InnateDB Gene IDBG-146556 (Ost4)
Protein Structure
UniProt Annotation
Function May be involved in N-glycosylation through its association with N-oligosaccharyl transferase. {ECO:0000250}.
Subcellular Localization Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III 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 4 interaction(s) predicted by orthology.
Predicted by orthology
Total 4 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
Biological Process
GO:0008150 biological_process
Cellular Component
GO:0005575 cellular_component
GO:0005789 endoplasmic reticulum membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1914945
InterPro IPR018943 Oligosaccaryltransferase
PFAM PF10215
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q99LX8
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 67695
UniGene
RefSeq NP_077780
MGI ID
MGI Symbol Ost4
OMIM
CCDS CCDS39049
HPRD
IMGT
EMBL AK002224 AK002453 AK003569 AK005413 AK010297 AK019285 BC002177 BC082316
GenPept AAH02177 AAH82316 BAC24992 BAC25041 BAC25115 BAC25288 BAC25588 BAE43146

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