CTU1_HUMAN
ID CTU1_HUMAN Reviewed; 348 AA.
AC Q7Z7A3; A8K558; Q96GZ7;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 1 {ECO:0000255|HAMAP-Rule:MF_03053};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_03053};
DE AltName: Full=ATP-binding domain-containing protein 3 {ECO:0000255|HAMAP-Rule:MF_03053};
DE AltName: Full=Cancer-associated gene protein;
DE AltName: Full=Cytoplasmic tRNA adenylyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN Name=CTU1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN Synonyms=ATPBD3 {ECO:0000255|HAMAP-Rule:MF_03053},
GN NCS6 {ECO:0000255|HAMAP-Rule:MF_03053};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yousef G.M., Borgono C.A., Davidian C.T., Michael I., Diamandis E.P.;
RT "Molecular characterization of a novel gene differentially expressed in
RT breast and prostate cancers.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-107.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP FUNCTION IN 2-THIOLATION OF TRNA, AND IDENTIFICATION IN A COMPLEX WITH URM1
RP AND CTU2.
RX PubMed=19017811; DOI=10.1073/pnas.0808756105;
RA Schlieker C.D., Van der Veen A.G., Damon J.R., Spooner E., Ploegh H.L.;
RT "A functional proteomics approach links the ubiquitin-related modifier Urm1
RT to a tRNA modification pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18255-18260(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds
CC tRNAs and probably acts by catalyzing adenylation of tRNAs, an
CC intermediate required for 2-thiolation. It is unclear whether it acts
CC as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1
CC onto the uridine of tRNAs at wobble position. {ECO:0000255|HAMAP-
CC Rule:MF_03053, ECO:0000269|PubMed:19017811}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03053}.
CC -!- SUBUNIT: Component of a complex at least composed of URM1, CTU2/NCS2
CC and CTU1/ATPBD3. May form a heterodimer with CTU2/NCS2.
CC {ECO:0000255|HAMAP-Rule:MF_03053, ECO:0000269|PubMed:19017811}.
CC -!- INTERACTION:
CC Q7Z7A3; Q9BTM9: URM1; NbExp=7; IntAct=EBI-15741880, EBI-714589;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03053}.
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DR EMBL; AY279382; AAP42277.1; -; Genomic_DNA.
DR EMBL; AK291173; BAF83862.1; -; mRNA.
DR EMBL; CH471135; EAW71984.1; -; Genomic_DNA.
DR EMBL; BC009037; AAH09037.1; -; mRNA.
DR CCDS; CCDS12824.1; -.
DR RefSeq; NP_660275.2; NM_145232.3.
DR AlphaFoldDB; Q7Z7A3; -.
DR SMR; Q7Z7A3; -.
DR BioGRID; 124701; 96.
DR DIP; DIP-48632N; -.
DR IntAct; Q7Z7A3; 20.
DR STRING; 9606.ENSP00000390011; -.
DR iPTMnet; Q7Z7A3; -.
DR PhosphoSitePlus; Q7Z7A3; -.
DR BioMuta; CTU1; -.
DR DMDM; 74713747; -.
DR EPD; Q7Z7A3; -.
DR jPOST; Q7Z7A3; -.
DR MassIVE; Q7Z7A3; -.
DR MaxQB; Q7Z7A3; -.
DR PaxDb; Q7Z7A3; -.
DR PeptideAtlas; Q7Z7A3; -.
DR PRIDE; Q7Z7A3; -.
DR ProteomicsDB; 69498; -.
DR Antibodypedia; 52772; 119 antibodies from 22 providers.
DR DNASU; 90353; -.
DR Ensembl; ENST00000421832.3; ENSP00000390011.1; ENSG00000142544.7.
DR GeneID; 90353; -.
DR KEGG; hsa:90353; -.
DR MANE-Select; ENST00000421832.3; ENSP00000390011.1; NM_145232.4; NP_660275.2.
DR UCSC; uc010eop.4; human.
DR CTD; 90353; -.
DR DisGeNET; 90353; -.
DR GeneCards; CTU1; -.
DR HGNC; HGNC:29590; CTU1.
DR HPA; ENSG00000142544; Low tissue specificity.
DR MIM; 612694; gene.
DR neXtProt; NX_Q7Z7A3; -.
DR OpenTargets; ENSG00000142544; -.
DR PharmGKB; PA165393368; -.
DR VEuPathDB; HostDB:ENSG00000142544; -.
DR eggNOG; KOG2840; Eukaryota.
DR GeneTree; ENSGT00390000001041; -.
DR HOGENOM; CLU_026481_1_2_1; -.
DR InParanoid; Q7Z7A3; -.
DR OMA; CLHINLG; -.
DR OrthoDB; 860739at2759; -.
DR PhylomeDB; Q7Z7A3; -.
DR TreeFam; TF352405; -.
DR BioCyc; MetaCyc:ENSG00000142544-MON; -.
DR PathwayCommons; Q7Z7A3; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q7Z7A3; -.
DR UniPathway; UPA00988; -.
DR BioGRID-ORCS; 90353; 379 hits in 1089 CRISPR screens.
DR GenomeRNAi; 90353; -.
DR Pharos; Q7Z7A3; Tbio.
DR PRO; PR:Q7Z7A3; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q7Z7A3; protein.
DR Bgee; ENSG00000142544; Expressed in thymus and 95 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0002144; C:cytosolic tRNA wobble base thiouridylase complex; IBA:GO_Central.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR GO; GO:0034227; P:tRNA thio-modification; NAS:UniProtKB.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; NAS:UniProtKB.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_03053; CTU1; 1.
DR InterPro; IPR032442; CTU1_C.
DR InterPro; IPR000541; Ncs6/Tuc1/Ctu1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011063; TilS/TtcA_N.
DR InterPro; IPR035107; tRNA_thiolation_TtcA_Ctu1.
DR PANTHER; PTHR11807:SF12; PTHR11807:SF12; 1.
DR Pfam; PF01171; ATP_bind_3; 1.
DR Pfam; PF16503; zn-ribbon_14; 1.
DR PIRSF; PIRSF004976; ATPase_YdaO; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding; Transferase;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..348
FT /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT /id="PRO_0000282391"
FT REGION 316..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 107
FT /note="A -> V (in dbSNP:rs17855403)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031402"
FT CONFLICT 71
FT /note="L -> R (in Ref. 4; AAH09037)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 36450 MW; 2BA258902B6CA142 CRC64;
MPAPPCASCH AARAALRRPL SGQALCGACF CAAFEAEVLH TVLAGRLLPP GAVVAVGASG
GKDSTVLAHV LRALAPRLGI SLQLVAVDEG IGGYRDAALA AVRRQAARWE LPLTVVAYED
LFGGWTMDAV ARSTAGSGRS RSCCTFCGVL RRRALEEGAR RVGATHIVTG HNADDMAETV
LMNFLRGDAG RLARGGGLGS PGEGGALPRC RPLQFASQKE VVLYAHFRRL DYFSEECVYA
PEAFRGHARD LLKRLEAARP SAVLDLVHSA ERLALAPAAR PPRPGACSRC GALASRALCQ
ACALLDGLNR GRPRLAIGKG RRGLDEEATP GTPGDPARPP ASKAVPTF
