Version 5.4
Mus musculus Protein: Dus3l
Summary
InnateDB Protein IDBP-192895.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Dus3l
Protein Name dihydrouridine synthase 3-like (S. cerevisiae)
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000007747
InnateDB Gene IDBG-192893 (Dus3l)
Protein Structure
UniProt Annotation
Function Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. {ECO:0000250}.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
They are also associated with 4 interaction(s) predicted by orthology.
Experimentally validated
Total 1 [view]
Protein-Protein 0
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 4 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0017150 tRNA dihydrouridine synthase activity
GO:0046872 metal ion binding
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0002943 tRNA dihydrouridine synthesis
GO:0008033 tRNA processing
GO:0055114 oxidation-reduction process
Cellular Component
GO:0005575 cellular_component
Protein Structure and Domains
PDB ID MGI:2147092
InterPro IPR001269 tRNA-dihydrouridine synthase
PFAM PF01207
PRINTS
PIRSF PIRSF006621
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q91XI1
PhosphoSite PhosphoSite-Q91XI1
TrEMBL
UniProt Splice Variant
Entrez Gene 224907
UniGene Mm.293973
RefSeq NP_659107
MGI ID
MGI Symbol Dus3l
OMIM
CCDS CCDS28914
HPRD
IMGT
EMBL AK157702 AY040840 BC052481
GenPept AAH52481 AAK84684 BAE34157

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