Version 5.4
Mus musculus Protein: Dalrd3
Summary
InnateDB Protein IDBP-200245.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Dalrd3
Protein Name DALR anticodon binding domain containing 3
Synonyms 6330580J24Rik; C77829;
Species Mus musculus
Ensembl Protein ENSMUSP00000019183
InnateDB Gene IDBG-200243 (Dalrd3)
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 0 experimentally validated interaction(s) in this database.
They are also associated with 4 interaction(s) predicted by orthology.
Predicted by orthology
Total 4 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004814 arginine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006420 arginyl-tRNA aminoacylation
GO:0008150 biological_process
Cellular Component
GO:0005575 cellular_component
Protein Structure and Domains
PDB ID MGI:1915039
InterPro IPR008909 DALR anticodon binding
IPR009080 Aminoacyl-tRNA synthetase, class 1a, anticodon-binding
PFAM PF05746
PRINTS
PIRSF
SMART SM00836
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q6PJN8
PhosphoSite PhosphoSite-Q6PJN8
TrEMBL
UniProt Splice Variant
Entrez Gene 67789
UniGene Mm.458081
RefSeq NP_080654
MGI ID
MGI Symbol Dalrd3
OMIM
CCDS CCDS40769
HPRD
IMGT
EMBL AK002439 AK003374 AK149963 AK169405 AK171818 BC013483
GenPept AAH13483 BAB22747 BAC24990 BAE29197 BAE41151 BAE42679

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