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Q99J10

- CTU1_MOUSE

UniProt

Q99J10 - CTU1_MOUSE

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

Organism-specific databases

MGIiMGI:2385277. Ctu1.

Subcellular locationi

Cytoplasm By similarity 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 1UniRule annotation
PRO_0000282392Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

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 By similarity.

Protein-protein interaction databases

BioGridi231384. 1 interaction.
STRINGi10090.ENSMUSP00000036770.

Structurei

3D structure databases

ProteinModelPortaliQ99J10.
SMRiQ99J10. Positions 54-236.

Family & Domainsi

Sequence similaritiesi

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

MPAPTCFSCH KTRAALRRPR SGQALCGSCF CAAFEAEVLH TVLAGHLLPP    50
GAVVAVGASG GKDSTVLAHV LRELAPRLGI TLHLVAVDEG IGGYRDAALE 100
AVRSQAARWE LPLTIVAYED LFGGWTMDAV ARSTAGSGRS RSCCTFCGVL 150
RRRALEEGAR LVGATHIVTG HNADDMAETV LMNFLRGDAG RLARGGVLGS 200
TGEGCALPRC RPLQFASQKE VVLYAHFRHL RYFSEECVYA PEAFRGHARD 250
LLKLLEAARP SAVLDLVHSA ERLALAPAAK PPPPGTCSRC GALASHKLCQ 300
ACALLDGLNR GLPRLAIGKG RRVLQVEPPQ PGNPSLVTSD PVAPAGPCTC 350
KQPKDKANPC GNGGDRAGAT CVSQCDLSPG NGEDRAGATC VSQRDLSLGN 400
GGDRAGATCV SQCDLSPVAE 420
Length:420
Mass (Da):43,823
Last modified:June 1, 2001 - v1
Checksum:i3DDCEDBE70D196B1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK155284 mRNA. Translation: BAE33164.1 .
BC005752 mRNA. Translation: AAH05752.1 .
CCDSi CCDS21179.1.
RefSeqi NP_663557.1. NM_145582.1.
UniGenei Mm.26514.

3D structure databases

ProteinModelPortali Q99J10.
SMRi Q99J10. Positions 54-236.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 231384. 1 interaction.
STRINGi 10090.ENSMUSP00000036770.

PTM databases

PhosphoSitei Q99J10.

Proteomic databases

PaxDbi Q99J10.
PRIDEi Q99J10.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000038332 ; ENSMUSP00000036770 ; ENSMUSG00000038888 .
GeneIDi 233189.
KEGGi mmu:233189.
UCSCi uc009gnh.1. mouse.

Organism-specific databases

CTDi 90353.
MGIi MGI:2385277. Ctu1.

Phylogenomic databases

eggNOGi COG0037.
GeneTreei ENSGT00390000001041.
HOGENOMi HOG000225864.
HOVERGENi HBG100428.
InParanoidi Q99J10.
KOi K14168.
OMAi ICTQGED.
OrthoDBi EOG7PGDRH.
PhylomeDBi Q99J10.
TreeFami TF352405.

Enzyme and pathway databases

UniPathwayi UPA00988 .

Miscellaneous databases

NextBioi 381599.
PROi Q99J10.
SOURCEi Search...

Gene expression databases

Bgeei Q99J10.
CleanExi MM_ATPBD3.
Genevestigatori Q99J10.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_03053. CTU1.
InterProi IPR000541. Ncs6/Tuc1/Ctu1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR011063. tRNA-lysidine/thiocyt_synth.
[Graphical view ]
Pfami PF01171. ATP_bind_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 93 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

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