Version 5.4
Homo sapiens Protein: CTU2
Summary
InnateDB Protein IDBP-381724.4
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol CTU2
Protein Name cytosolic thiouridylase subunit 2 homolog (S. pombe)
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000388320
InnateDB Gene IDBG-46510 (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, ECO:0000269PubMed:19017811}.
Subcellular Localization Cytoplasm.
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.
Experimentally validated
Total 7 [view]
Protein-Protein 7 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0000049 tRNA binding
GO:0005515 protein binding
GO:0016779 nucleotidyltransferase activity
Biological Process
GO:0002098 tRNA wobble uridine modification
GO:0032447 protein urmylation
GO:0034227 tRNA thio-modification
Cellular Component
GO:0005737 cytoplasm
GO:0043234 protein complex
Protein Structure and Domains
PDB ID
InterPro IPR019407 Thiouridylase, cytoplasmic, subunit 2
PFAM PF10288
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q2VPK5
PhosphoSite PhosphoSite-Q2VPK5
TrEMBL H3BNU5
UniProt Splice Variant
Entrez Gene 348180
UniGene Hs.592074
RefSeq NP_001012777
HUGO HGNC:28005
OMIM
CCDS CCDS45545
HPRD 18372
IMGT
EMBL AC138028 AK299521 BC021829 BC080540 BC108659 BC121805 BC125269 BC157881
GenPept AAH80540 AAI08660 AAI21806 AAI25270 AAI57882 BAG61472

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