Version 5.4
Homo sapiens Protein: CTU1
Summary
InnateDB Protein IDBP-384023.4
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol CTU1
Protein Name cytosolic thiouridylase subunit 1 homolog (S. pombe)
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000390011
InnateDB Gene IDBG-65655 (CTU1)
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). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. {ECO:0000255HAMAP-Rule:MF_03053, 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 11 experimentally validated interaction(s) in this database.
Experimentally validated
Total 11 [view]
Protein-Protein 11 [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:0008033 tRNA processing
GO:0032447 protein urmylation
GO:0034227 tRNA thio-modification
Cellular Component
GO:0005739 mitochondrion
GO:0005829 cytosol
Protein Structure and Domains
PDB ID
InterPro IPR011063 tRNA(Ile)-lysidine/2-thiocytidine synthase
IPR012089 2-thiocytidine tRNA biosynthesis protein, TtcA
PFAM PF01171
PRINTS
PIRSF PIRSF004976
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q7Z7A3
PhosphoSite PhosphoSite-Q7Z7A3
TrEMBL
UniProt Splice Variant
Entrez Gene 90353
UniGene Hs.148425
RefSeq NP_660275
HUGO HGNC:29590
OMIM 612694
CCDS CCDS12824
HPRD 14270
IMGT
EMBL AK291173 AY279382 BC009037 CH471135
GenPept AAH09037 AAP42277 BAF83862 EAW71984

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