Version 5.4
Mus musculus Protein: Ola1
Summary
InnateDB Protein IDBP-256809.5
Last Modified 2012-02-14 [Report errors or provide feedback]
Gene Symbol Ola1
Protein Name Obg-like ATPase 1
Synonyms 2510025G09Rik; 2810405J23Rik; 2810409H07Rik; Gtpbp9; PTD004;
Species Mus musculus
Ensembl Protein ENSMUSP00000107686
InnateDB Gene IDBG-179846 (Ola1)
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 7 experimentally validated interaction(s) in this database.
They are also associated with 16 interaction(s) predicted by orthology.
Experimentally validated
Total 7 [view]
Protein-Protein 7 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 16 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005525 GTP binding
GO:0015093 ferrous iron transmembrane transporter activity
Biological Process
GO:0015684 ferrous iron transport
Cellular Component
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1914309
InterPro IPR006073 GTP binding domain
IPR011619 Ferrous iron transport protein B, N-terminal
IPR027417 P-loop containing nucleoside triphosphate hydrolase
PFAM PF01926
PF02421
PRINTS PR00326
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-
TrEMBL B1AYJ9
UniProt Splice Variant
Entrez Gene 67059
UniGene Mm.468127
RefSeq
MGI ID
MGI Symbol Ola1
OMIM
CCDS
HPRD
IMGT
EMBL AL928608 BX284615
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