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Search results 1 to 72 out of 72 for Ctu2

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Type Details Score
Gene
Type: gene
Organism: human
Gene
Type: gene
Organism: cattle
Gene
Type: gene
Organism: chicken
Gene
Type: gene
Organism: zebrafish
Gene
Type: gene
Organism: macaque, rhesus
Gene
Type: gene
Organism: frog, western clawed
Gene
Type: gene
Organism: frog, African clawed
Gene
Type: gene
Organism: rat
Gene
Type: gene
Organism: dog, domestic
Gene
Type: gene
Organism: chimpanzee
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Domain
Type: Family
Description: Cytoplasmic tRNA 2-thiolation protein 2 (also known as Ncs2/Tuc2 in budding yeasts) is responsible for 2-thiolation of mcm5S2U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln) [, ]. Its fission yeast homologue, Ctu2 forms a complex with Ctu1 (Ncs6/Tuc1 homologue) and serves as a putative enzyme for the formation of 2-thiouridine [].
Protein
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
Publication
First Author: Dewez M
Year: 2008
Journal: Proc Natl Acad Sci U S A
Title: The conserved Wobble uridine tRNA thiolase Ctu1-Ctu2 is required to maintain genome integrity.
Volume: 105
Issue: 14
Pages: 5459-64
Publication
First Author: Nakai Y
Year: 2008
Journal: J Biol Chem
Title: Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems.
Volume: 283
Issue: 41
Pages: 27469-76
Protein
Organism: Mus musculus/domesticus
Length: 514  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 249  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 111  
Fragment?: true
Publication
First Author: Noma A
Year: 2009
Journal: Nucleic Acids Res
Title: Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions.
Volume: 37
Issue: 4
Pages: 1335-52
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus pahari
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus spretus
GXD Expression  
Probe: MGI:3526268
Assay Type: RNA in situ
Annotation Date: 2005-02-14
Strength: Present
Sex: Male
Emaps: EMAPS:2909821
Pattern: Not Specified
Stage: TS21
Assay Id: MGI:3526332
Age: embryonic day 12.5
Image: left gonad, male
Specimen Label: left gonad, male
Detected: true
Specimen Num: 1
GXD Expression  
Probe: MGI:3526268
Assay Type: RNA in situ
Annotation Date: 2005-02-14
Strength: Present
Sex: Female
Emaps: EMAPS:1796221
Pattern: Not Specified
Stage: TS21
Assay Id: MGI:3526332
Age: embryonic day 12.5
Image: right gonad, female
Specimen Label: right gonad, female
Detected: true
Specimen Num: 2
Publication
First Author: McClive PJ
Year: 2003
Journal: Genesis
Title: Subtractive hybridisation screen identifies sexually dimorphic gene expression in the embryonic mouse gonad.
Volume: 37
Issue: 2
Pages: 84-90
Publication        
First Author: UniProt curators
Year: 2014
Title: Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Publication      
First Author: International Mouse Strain Resource
Year: 2014
Journal: Database Download
Title: MGI download of germline transmission data for alleles from IMSR strain data
Publication      
First Author: Wellcome Trust Sanger Institute
Year: 2009
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by the Wellcome Trust Sanger Institute
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: Gene Ontology Annotation by the MGI Curatorial Staff
Publication      
First Author: Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC)
Year: 2014
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database
Publication        
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Publication
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
Publication
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
Publication        
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
Publication
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
Publication        
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Publication
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
Publication
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication        
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Protein Domain
Type: Family
Description: Cytoplasmic tRNA 2-thiolation protein 1 (also known as Ncs6/Tuc1 in budding yeasts) is responsible for 2-thiolation of mcm5S2U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln) [, ]. It directly bind tRNAs and probably acts by catalysing adenylation of tRNAs, an intermediate required for 2-thiolation. Its fission yeast homologue, Ctu1 forms a complex with Ctu2 (Ncs2/Tuc2 homologue) and serves as a putative enzyme for the formation of 2-thiouridine []. This family also includes tRNA-5-methyluridine(54) 2-sulfurtransferase, which catalyzes the 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine [].
Publication
First Author: Arragain S
Year: 2017
Journal: Proc Natl Acad Sci U S A
Title: Nonredox thiolation in tRNA occurring via sulfur activation by a [4Fe-4S] cluster.
Volume: 114
Issue: 28
Pages: 7355-7360
Protein
Organism: Mus musculus/domesticus
Length: 420  
Fragment?: false
Protein Domain
Type: Family
Description: This entry represents a group of tRNA thiolation proteins. It includes the tRNA-cytidine(32) 2-sulfurtransferase (), and Cytoplasmic tRNA 2-thiolation protein 1 ().tRNA-cytidine(32) 2-sulfurtransferase (also known as 2-thiocytidine tRNA biosynthesis protein TtcA) is required for the thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The modified nucleoside 2-thiocytidine (s(2)C) has so far been found in tRNA from archaea and bacteria. The TtcA protein family is characterised by the existence of both a PP-loop and a Cys-X(1)-X(2)-Cys motif in the central region of the protein but can be divided into two distinct groups based on the presence and location of additional Cys-X(1)-X(2)-Cys motifs in terminal regions of the sequence. Mutant analysis showed that both cysteines in this central conserved Cys-X(1)-X(2)-Cys motif are required for the formation of s(2)C []. The PP-loop motif appears to be a modified version of the P-loop of nucleotide binding domain that is involved in phosphate binding []. Named PP-motif, since it appears to be a part of a previously uncharacterised ATP pyrophophatase domain. ATP sulfurylases, Escherichia coli NtrL, and Bacillus subtilis OutB consist of this domain alone. In other proteins, the pyrophosphatase domain is associated with amidotransferase domains (type I or type II), a putative citrulline-aspartate ligase domain or a nitrilase/amidase domain.Cytoplasmic tRNA 2-thiolation protein 1 (also known as Ncs6/Tuc1 in budding yeasts) is responsible for 2-thiolation of mcm5S2U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln) [, ]. It directly bind tRNAs and probably acts by catalysing adenylation of tRNAs, an intermediate required for 2-thiolation. Its fission yeast homologue, Ctu1 forms a complex with Ctu2 (Ncs2/Tuc2 homologue) and serves as a putative enzyme for the formation of 2-thiouridine []. This family also includes tRNA-5-methyluridine(54) 2-sulfurtransferase, which catalyzes the 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine [].
Publication
First Author: Jäger G
Year: 2004
Journal: J Bacteriol
Title: The conserved Cys-X1-X2-Cys motif present in the TtcA protein is required for the thiolation of cytidine in position 32 of tRNA from Salmonella enterica serovar Typhimurium.
Volume: 186
Issue: 3
Pages: 750-7
Publication
First Author: Bork P
Year: 1994
Journal: Proteins
Title: A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity.
Volume: 20
Issue: 4
Pages: 347-55