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Protein

Cytoplasmic tRNA 2-thiolation protein 1

Gene

CTU1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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 annotation1 Publication

Pathway: 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis

This protein is involved in the pathway 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis, which is part of tRNA modification.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis and in tRNA modification.

GO - Molecular functioni

GO - Biological processi

  • protein urmylation Source: UniProtKB-HAMAP
  • tRNA thio-modification Source: UniProtKB
  • 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
Cancer-associated gene protein
Cytoplasmic tRNA adenylyltransferase 1UniRule annotation
Gene namesi
Name:CTU1UniRule annotation
Synonyms:ATPBD3UniRule annotation, NCS6UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:29590. CTU1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165393368.

Polymorphism and mutation databases

BioMutaiCTU1.
DMDMi74713747.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348Cytoplasmic tRNA 2-thiolation protein 1PRO_0000282391Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei200 – 2001Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ7Z7A3.
PaxDbiQ7Z7A3.
PRIDEiQ7Z7A3.

PTM databases

PhosphoSiteiQ7Z7A3.

Expressioni

Gene expression databases

BgeeiQ7Z7A3.
CleanExiHS_ATPBD3.

Organism-specific databases

HPAiHPA053797.

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 annotation1 Publication

Protein-protein interaction databases

BioGridi124701. 17 interactions.
DIPiDIP-48632N.
STRINGi9606.ENSP00000390011.

Structurei

3D structure databases

ProteinModelPortaliQ7Z7A3.
SMRiQ7Z7A3. Positions 46-254.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0037.
GeneTreeiENSGT00390000001041.
HOGENOMiHOG000225864.
HOVERGENiHBG100428.
InParanoidiQ7Z7A3.
KOiK14168.
OMAiICTQGED.
OrthoDBiEOG7PGDRH.
PhylomeDBiQ7Z7A3.
TreeFamiTF352405.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_03053. CTU1.
InterProiIPR012089. 2-thiocytidine_tRNA_synth_TtcA.
IPR000541. 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]
PIRSFiPIRSF004976. ATPase_YdaO. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7Z7A3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAPPCASCH AARAALRRPL SGQALCGACF CAAFEAEVLH TVLAGRLLPP
60 70 80 90 100
GAVVAVGASG GKDSTVLAHV LRALAPRLGI SLQLVAVDEG IGGYRDAALA
110 120 130 140 150
AVRRQAARWE LPLTVVAYED LFGGWTMDAV ARSTAGSGRS RSCCTFCGVL
160 170 180 190 200
RRRALEEGAR RVGATHIVTG HNADDMAETV LMNFLRGDAG RLARGGGLGS
210 220 230 240 250
PGEGGALPRC RPLQFASQKE VVLYAHFRRL DYFSEECVYA PEAFRGHARD
260 270 280 290 300
LLKRLEAARP SAVLDLVHSA ERLALAPAAR PPRPGACSRC GALASRALCQ
310 320 330 340
ACALLDGLNR GRPRLAIGKG RRGLDEEATP GTPGDPARPP ASKAVPTF
Length:348
Mass (Da):36,450
Last modified:October 1, 2003 - v1
Checksum:i2BA258902B6CA142
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711L → R in AAH09037 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071A → V.1 Publication
Corresponds to variant rs17855403 [ dbSNP | Ensembl ].
VAR_031402

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY279382 Genomic DNA. Translation: AAP42277.1.
AK291173 mRNA. Translation: BAF83862.1.
CH471135 Genomic DNA. Translation: EAW71984.1.
BC009037 mRNA. Translation: AAH09037.1.
CCDSiCCDS12824.1.
RefSeqiNP_660275.2. NM_145232.3.
UniGeneiHs.148425.

Genome annotation databases

EnsembliENST00000421832; ENSP00000390011; ENSG00000142544.
GeneIDi90353.
KEGGihsa:90353.
UCSCiuc010eop.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY279382 Genomic DNA. Translation: AAP42277.1.
AK291173 mRNA. Translation: BAF83862.1.
CH471135 Genomic DNA. Translation: EAW71984.1.
BC009037 mRNA. Translation: AAH09037.1.
CCDSiCCDS12824.1.
RefSeqiNP_660275.2. NM_145232.3.
UniGeneiHs.148425.

3D structure databases

ProteinModelPortaliQ7Z7A3.
SMRiQ7Z7A3. Positions 46-254.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124701. 17 interactions.
DIPiDIP-48632N.
STRINGi9606.ENSP00000390011.

PTM databases

PhosphoSiteiQ7Z7A3.

Polymorphism and mutation databases

BioMutaiCTU1.
DMDMi74713747.

Proteomic databases

MaxQBiQ7Z7A3.
PaxDbiQ7Z7A3.
PRIDEiQ7Z7A3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000421832; ENSP00000390011; ENSG00000142544.
GeneIDi90353.
KEGGihsa:90353.
UCSCiuc010eop.3. human.

Organism-specific databases

CTDi90353.
GeneCardsiGC19M051601.
H-InvDBHIX0015377.
HIX0137480.
HGNCiHGNC:29590. CTU1.
HPAiHPA053797.
MIMi612694. gene.
neXtProtiNX_Q7Z7A3.
PharmGKBiPA165393368.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0037.
GeneTreeiENSGT00390000001041.
HOGENOMiHOG000225864.
HOVERGENiHBG100428.
InParanoidiQ7Z7A3.
KOiK14168.
OMAiICTQGED.
OrthoDBiEOG7PGDRH.
PhylomeDBiQ7Z7A3.
TreeFamiTF352405.

Enzyme and pathway databases

UniPathwayiUPA00988.

Miscellaneous databases

GenomeRNAii90353.
NextBioi76697.
PROiQ7Z7A3.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z7A3.
CleanExiHS_ATPBD3.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_03053. CTU1.
InterProiIPR012089. 2-thiocytidine_tRNA_synth_TtcA.
IPR000541. 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]
PIRSFiPIRSF004976. ATPase_YdaO. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of a novel gene differentially expressed in breast and prostate cancers."
    Yousef G.M., Borgono C.A., Davidian C.T., Michael I., Diamandis E.P.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Teratocarcinoma.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANT VAL-107.
    Tissue: Brain.
  5. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway."
    Schlieker C.D., Van der Veen A.G., Damon J.R., Spooner E., Ploegh H.L.
    Proc. Natl. Acad. Sci. U.S.A. 105:18255-18260(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN 2-THIOLATION OF TRNA, IDENTIFICATION IN A COMPLEX WITH URM1 AND CTU2.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiCTU1_HUMAN
AccessioniPrimary (citable) accession number: Q7Z7A3
Secondary accession number(s): A8K558, Q96GZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 1, 2003
Last modified: June 24, 2015
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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.