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Protein

Cytoplasmic tRNA 2-thiolation protein 1

Gene

Ctu1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Plays a central role in 2-thiolation of mcm5S2U 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.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. nucleotidyltransferase activity Source: UniProtKB-HAMAP
  2. tRNA binding Source: UniProtKB

GO - Biological processi

  1. protein urmylation Source: UniProtKB-HAMAP
  2. tRNA thio-modification Source: UniProtKB
  3. tRNA wobble uridine modification Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

RNA-binding, tRNA-binding

Enzyme and pathway databases

UniPathwayiUPA00988.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic tRNA 2-thiolation protein 1UniRule annotation (EC:2.7.7.-UniRule annotation)
Alternative name(s):
ATP-binding domain-containing protein 3UniRule annotation
Cytoplasmic tRNA adenylyltransferase 1UniRule annotation
Gene namesi
Name:Ctu1
Synonyms:Atpbd3, Ncs6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2385277. Ctu1.

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 420420Cytoplasmic tRNA 2-thiolation protein 1PRO_0000282392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei200 – 2001PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ99J10.
PaxDbiQ99J10.
PRIDEiQ99J10.

PTM databases

PhosphoSiteiQ99J10.

Expressioni

Gene expression databases

BgeeiQ99J10.
CleanExiMM_ATPBD3.
GenevestigatoriQ99J10.

Interactioni

Subunit structurei

Component of a complex at least composed of URM1, CTU2/NCS2 and CTU1/ATPBD3. May form a heterodimer with CTU2/NCS2.UniRule annotation

Protein-protein interaction databases

BioGridi231384. 1 interaction.
STRINGi10090.ENSMUSP00000036770.

Structurei

3D structure databases

ProteinModelPortaliQ99J10.
SMRiQ99J10. Positions 54-236.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0037.
GeneTreeiENSGT00390000001041.
HOGENOMiHOG000225864.
HOVERGENiHBG100428.
InParanoidiQ99J10.
KOiK14168.
OMAiICTQGED.
OrthoDBiEOG7PGDRH.
PhylomeDBiQ99J10.
TreeFamiTF352405.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_03053. CTU1.
InterProiIPR000541. Ncs6/Tuc1/Ctu1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR011063. tRNA-lysidine/thiocyt_synth.
[Graphical view]
PfamiPF01171. ATP_bind_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99J10-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAPTCFSCH KTRAALRRPR SGQALCGSCF CAAFEAEVLH TVLAGHLLPP
60 70 80 90 100
GAVVAVGASG GKDSTVLAHV LRELAPRLGI TLHLVAVDEG IGGYRDAALE
110 120 130 140 150
AVRSQAARWE LPLTIVAYED LFGGWTMDAV ARSTAGSGRS RSCCTFCGVL
160 170 180 190 200
RRRALEEGAR LVGATHIVTG HNADDMAETV LMNFLRGDAG RLARGGVLGS
210 220 230 240 250
TGEGCALPRC RPLQFASQKE VVLYAHFRHL RYFSEECVYA PEAFRGHARD
260 270 280 290 300
LLKLLEAARP SAVLDLVHSA ERLALAPAAK PPPPGTCSRC GALASHKLCQ
310 320 330 340 350
ACALLDGLNR GLPRLAIGKG RRVLQVEPPQ PGNPSLVTSD PVAPAGPCTC
360 370 380 390 400
KQPKDKANPC GNGGDRAGAT CVSQCDLSPG NGEDRAGATC VSQRDLSLGN
410 420
GGDRAGATCV SQCDLSPVAE
Length:420
Mass (Da):43,823
Last modified:June 1, 2001 - v1
Checksum:i3DDCEDBE70D196B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK155284 mRNA. Translation: BAE33164.1.
BC005752 mRNA. Translation: AAH05752.1.
CCDSiCCDS21179.1.
RefSeqiNP_663557.1. NM_145582.1.
UniGeneiMm.26514.

Genome annotation databases

EnsembliENSMUST00000038332; ENSMUSP00000036770; ENSMUSG00000038888.
GeneIDi233189.
KEGGimmu:233189.
UCSCiuc009gnh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK155284 mRNA. Translation: BAE33164.1.
BC005752 mRNA. Translation: AAH05752.1.
CCDSiCCDS21179.1.
RefSeqiNP_663557.1. NM_145582.1.
UniGeneiMm.26514.

3D structure databases

ProteinModelPortaliQ99J10.
SMRiQ99J10. Positions 54-236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231384. 1 interaction.
STRINGi10090.ENSMUSP00000036770.

PTM databases

PhosphoSiteiQ99J10.

Proteomic databases

MaxQBiQ99J10.
PaxDbiQ99J10.
PRIDEiQ99J10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038332; ENSMUSP00000036770; ENSMUSG00000038888.
GeneIDi233189.
KEGGimmu:233189.
UCSCiuc009gnh.1. mouse.

Organism-specific databases

CTDi90353.
MGIiMGI:2385277. Ctu1.

Phylogenomic databases

eggNOGiCOG0037.
GeneTreeiENSGT00390000001041.
HOGENOMiHOG000225864.
HOVERGENiHBG100428.
InParanoidiQ99J10.
KOiK14168.
OMAiICTQGED.
OrthoDBiEOG7PGDRH.
PhylomeDBiQ99J10.
TreeFamiTF352405.

Enzyme and pathway databases

UniPathwayiUPA00988.

Miscellaneous databases

NextBioi381599.
PROiQ99J10.
SOURCEiSearch...

Gene expression databases

BgeeiQ99J10.
CleanExiMM_ATPBD3.
GenevestigatoriQ99J10.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_03053. CTU1.
InterProiIPR000541. Ncs6/Tuc1/Ctu1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR011063. tRNA-lysidine/thiocyt_synth.
[Graphical view]
PfamiPF01171. ATP_bind_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NMRI.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiCTU1_MOUSE
AccessioniPrimary (citable) accession number: Q99J10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.