Version 5.4
Mus musculus Protein: Osbpl3
Summary
InnateDB Protein IDBP-146880.5
Last Modified 2012-02-14 [Report errors or provide feedback]
Gene Symbol Osbpl3
Protein Name oxysterol binding protein-like 3
Synonyms 1200014M06Rik; 6720421I08Rik; A530055M08; ORP3; OSBP3;
Species Mus musculus
Ensembl Protein ENSMUSP00000071643
InnateDB Gene IDBG-146878 (Osbpl3)
Protein Structure
UniProt Annotation
Function
Subcellular Localization
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 5 interaction(s) predicted by orthology.
Experimentally validated
Total 2 [view]
Protein-Protein 1 [view]
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 5 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0015485 cholesterol binding
Biological Process
GO:0006869 lipid transport
GO:0008150 biological_process
Cellular Component
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0031965 nuclear membrane
GO:0097038 perinuclear endoplasmic reticulum
Protein Structure and Domains
PDB ID MGI:1918970
InterPro IPR000648 Oxysterol-binding protein
IPR001849 Pleckstrin homology domain
PFAM PF01237
PF00169
PRINTS
PIRSF
SMART SM00233
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-
TrEMBL F8WH20
UniProt Splice Variant
Entrez Gene 71720
UniGene Mm.472621
RefSeq NP_001157117
MGI ID
MGI Symbol Osbpl3
OMIM
CCDS CCDS51771
HPRD
IMGT
EMBL AC008160 AC124689
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