Version 5.4
Mus musculus Protein: Mrs2
Summary
InnateDB Protein IDBP-139588.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Mrs2
Protein Name MRS2 magnesium homeostasis factor homolog (S. cerevisiae)
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000021772
InnateDB Gene IDBG-139586 (Mrs2)
Protein Structure
UniProt Annotation
Function Magnesium transporter that may mediate the influx of magnesium into the mitochondrial matrix. {ECO:0000250}.
Subcellular Localization Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Disease Associations
Tissue Specificity Ubiquitously expressed. {ECO:0000269PubMed:11401429}.
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 1 interaction(s) predicted by orthology.
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0015095 magnesium ion transmembrane transporter activity
Biological Process
GO:0008150 biological_process
GO:0015693 magnesium ion transport
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:2685748
InterPro
PFAM
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q5NCE8
PhosphoSite PhosphoSite-NP_001013407
TrEMBL
UniProt Splice Variant
Entrez Gene 380836
UniGene Mm.387097
RefSeq NP_001013407
MGI ID
MGI Symbol Mrs2
OMIM
CCDS
HPRD
IMGT
EMBL AL645533
GenPept CAI35077

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