Version 5.4
Mus musculus Protein: Ctu2
Summary
InnateDB Protein IDBP-274190.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ctu2
Protein Name cytosolic thiouridylase subunit 2 homolog (S. pombe)
Synonyms 2310061F22Rik; C16orf84; Ncs2;
Species Mus musculus
Ensembl Protein ENSMUSP00000112113
InnateDB Gene IDBG-197398 (Ctu2)
Protein Structure
UniProt Annotation
Function Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with CTU1/ATPBD3 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. {ECO:0000255HAMAP-Rule:MF_03054}.
Subcellular Localization Cytoplasm {ECO:0000255HAMAP-Rule:MF_03054}.
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 3 interaction(s) predicted by orthology.
Predicted by orthology
Total 3 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000049 tRNA binding
GO:0003674 molecular_function
GO:0005515 protein binding
GO:0016779 nucleotidyltransferase activity
Biological Process
GO:0002098 tRNA wobble uridine modification
GO:0008150 biological_process
GO:0032447 protein urmylation
GO:0034227 tRNA thio-modification
Cellular Component
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0043234 protein complex
Protein Structure and Domains
PDB ID MGI:1914215
InterPro IPR019407 Thiouridylase, cytoplasmic, subunit 2
PFAM PF10288
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q3U308
PhosphoSite PhosphoSite-Q3U308
TrEMBL
UniProt Splice Variant
Entrez Gene 66965
UniGene
RefSeq NP_722470
MGI ID
MGI Symbol Ctu2
OMIM
CCDS CCDS52694
HPRD
IMGT
EMBL AK090349 AK154995 BC036332
GenPept AAH36332 BAC41181 BAE32982

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