Q7Z7A3 (CTU1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytoplasmic tRNA 2-thiolation protein 1
EC=2.7.7.-

Alternative name(s):
ATP-binding domain-containing protein 3
Cancer-associated gene protein
Cytoplasmic tRNA adenylyltransferase 1

Gene names

Name:	CTU1
Synonyms:	ATPBD3, NCS6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8
Pathway	tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Subunit structure	Component of a complex at least composed of URM1, CTU2/NCS2 and CTU1/ATPBD3. May form a heterodimer with CTU2/NCS2. Ref.8
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	RNA-binding tRNA-binding
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	tRNA thio-modification Non-traceable author statement Ref.8. Source: UniProtKB tRNA wobble uridine modification Non-traceable author statement Ref.8. Source: UniProtKB
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 348	348	Cytoplasmic tRNA 2-thiolation protein 1		PRO_0000282391
Amino acid modifications
	Modified residue	200	1	Phosphoserine Ref.5 Ref.6 Ref.9
Natural variations
	Natural variant	107	1	A → V. Ref.4 Corresponds to variant rs17855403 [ dbSNP | Ensembl ].		VAR_031402
Experimental info
	Sequence conflict	71	1	L → R in AAH09037. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q7Z7A3 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 2BA258902B6CA142	FASTA	348	36,450
	10 20 30 40 50 60 MPAPPCASCH AARAALRRPL SGQALCGACF CAAFEAEVLH TVLAGRLLPP GAVVAVGASG 70 80 90 100 110 120 GKDSTVLAHV LRALAPRLGI SLQLVAVDEG IGGYRDAALA AVRRQAARWE LPLTVVAYED 130 140 150 160 170 180 LFGGWTMDAV ARSTAGSGRS RSCCTFCGVL RRRALEEGAR RVGATHIVTG HNADDMAETV 190 200 210 220 230 240 LMNFLRGDAG RLARGGGLGS PGEGGALPRC RPLQFASQKE VVLYAHFRRL DYFSEECVYA 250 260 270 280 290 300 PEAFRGHARD LLKRLEAARP SAVLDLVHSA ERLALAPAAR PPRPGACSRC GALASRALCQ 310 320 330 340 ACALLDGLNR GRPRLAIGKG RRGLDEEATP GTPGDPARPP ASKAVPTF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY279382 Genomic DNA. Translation: AAP42277.1. AK291173 mRNA. Translation: BAF83862.1. CH471135 Genomic DNA. Translation: EAW71984.1. BC009037 mRNA. Translation: AAH09037.1.
IPI	IPI00062882.
RefSeq	NP_660275.2. NM_145232.3.
UniGene	Hs.148425.
3D structure databases
ProteinModelPortal	Q7Z7A3.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48632N.
STRING	9606.ENSP00000270637.
PTM databases
PhosphoSite	Q7Z7A3.
Polymorphism databases
DMDM	74713747.
Proteomic databases
PaxDb	Q7Z7A3.
PRIDE	Q7Z7A3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000421832; ENSP00000390011; ENSG00000142544.
GeneID	90353.
KEGG	hsa:90353.
UCSC	uc010eop.3. human.
Organism-specific databases
CTD	90353.
GeneCards	GC19M051601.
H-InvDB	HIX0015377. HIX0137480.
HGNC	HGNC:29590. CTU1.
HPA	HPA053797.
MIM	612694. gene.
neXtProt	NX_Q7Z7A3.
PharmGKB	PA165393368.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0037.
HOGENOM	HOG000225864.
HOVERGEN	HBG100428.
InParanoid	Q7Z7A3.
KO	K14168.
OMA	YEELYGW.
OrthoDB	EOG4SBF02.
Enzyme and pathway databases
UniPathway	UPA00988.
Gene expression databases
Bgee	Q7Z7A3.
CleanEx	HS_ATPBD3.
Genevestigator	Q7Z7A3.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
InterPro	IPR012089. 2-thiocytidine_tRNA_synth_TtcA. IPR014729. Rossmann-like_a/b/a_fold. IPR011063. tRNA-lysidine/thiocyt_synth. [Graphical view]
Pfam	PF01171. ATP_bind_3. 1 hit. [Graphical view]
PIRSF	PIRSF004976. ATPase_YdaO. 1 hit.
PROSITE	PS01263. UPF0021. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	90353.
NextBio	76697.
SOURCE	Search...

Entry information

Entry name

CTU1_HUMAN

Accession

Primary (citable) accession number: Q7Z7A3
Secondary accession number(s): A8K558, Q96GZ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	October 1, 2003
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.