Version 5.4
Mus musculus Protein: Dus4l
Summary
InnateDB Protein IDBP-133548.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Dus4l
Protein Name dihydrouridine synthase 4-like (S. cerevisiae)
Synonyms 2310069P03Rik; 2700089B10Rik; AI482040; Pp35;
Species Mus musculus
Ensembl Protein ENSMUSP00000020977
InnateDB Gene IDBG-133546 (Dus4l)
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 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:0017150 tRNA dihydrouridine synthase activity
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:1919166
InterPro IPR001269 tRNA-dihydrouridine synthase
PFAM PF01207
PRINTS
PIRSF PIRSF006621
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q32M08
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 71916
UniGene Mm.62979
RefSeq NP_082278
MGI ID
MGI Symbol Dus4l
OMIM
CCDS CCDS25865
HPRD
IMGT
EMBL AK010138 BC109351
GenPept AAI09352 BAB26724

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