Version 5.4
Mus musculus Protein: BC003331
Summary
InnateDB Protein IDBP-197410.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol BC003331
Protein Name cDNA sequence BC003331
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000092050
InnateDB Gene IDBG-197406 (BC003331)
Protein Structure
UniProt Annotation
Function May play a role in the trafficking of a subset of G- protein coupled receptors. {ECO:0000250}.
Subcellular Localization Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Disease Associations
Tissue Specificity Ubiquitously expressed. {ECO:0000269PubMed:15718105}.
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 2 interaction(s) predicted by orthology.
Predicted by orthology
Total 2 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
Biological Process
GO:0008150 biological_process
GO:0055114 oxidation-reduction process
Cellular Component
GO:0005575 cellular_component
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:2385108
InterPro
PFAM
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q4PJX1
PhosphoSite PhosphoSite-Q4PJX1
TrEMBL
UniProt Splice Variant
Entrez Gene 226499
UniGene Mm.400816
RefSeq
MGI ID
MGI Symbol BC003331
OMIM
CCDS
HPRD
IMGT
EMBL AK152022 BC003331 DQ077804
GenPept AAH03331 AAY83272 BAE30884

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