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tRNA-dihydrouridine(20) synthase [NAD(P) ]-like (EC 1.3.1.-) (Dihydrouridine synthase 2) (Up-regulated in lung cancer protein 8) (URLC8) (tRNA-dihydrouridine synthase 2-like) (hDUS2)

 DUS2L_HUMAN             Reviewed;         493 AA.
Q9NX74; A8K3G3; Q4H4D9;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
12-SEP-2018, entry version 138.
RecName: Full=tRNA-dihydrouridine(20) synthase [NAD(P)+]-like;
EC=1.3.1.-;
AltName: Full=Dihydrouridine synthase 2;
AltName: Full=Up-regulated in lung cancer protein 8;
Short=URLC8;
AltName: Full=tRNA-dihydrouridine synthase 2-like;
Short=hDUS2;
Name=DUS2; Synonyms=DUS2L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INTERACTION WITH EPRS.
PubMed=15994936; DOI=10.1158/0008-5472.CAN-05-0600;
Kato T., Daigo Y., Hayama S., Ishikawa N., Yamabuki T., Ito T.,
Miyamoto M., Kondo S., Nakamura Y.;
"A novel human tRNA-dihydrouridine synthase involved in pulmonary
carcinogenesis.";
Cancer Res. 65:5638-5646(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Gastric carcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, AND INTERACTION WITH PRKRA AND EIF2AK2.
PubMed=18096616; DOI=10.1093/nar/gkm1129;
Mittelstadt M., Frump A., Khuu T., Fowlkes V., Handy I., Patel C.V.,
Patel R.C.;
"Interaction of human tRNA-dihydrouridine synthase-2 with interferon-
induced protein kinase PKR.";
Nucleic Acids Res. 36:998-1008(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445 AND SER-488, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Dihydrouridine synthase. Catalyzes the synthesis of
dihydrouridine, a modified base found in the D-loop of most tRNAs.
Negatively regulates the activation of EIF2AK2/PKR.
{ECO:0000269|PubMed:15994936, ECO:0000269|PubMed:18096616}.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000250|UniProtKB:Q5SMC7};
-!- SUBUNIT: Interacts with EPRS. Interacts (via DRBM domain) with
PRKRA and EIF2AK2/PKR (via DRBM 1 domain).
{ECO:0000269|PubMed:15994936, ECO:0000269|PubMed:18096616}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15994936}.
Endoplasmic reticulum {ECO:0000269|PubMed:15994936}. Note=Mainly
at the endoplasmic reticulum.
-!- TISSUE SPECIFICITY: Weak expression in heart, placenta and
skeletal muscle. Up-regulated in most lung cancer cells (at
protein level). {ECO:0000269|PubMed:15994936}.
-!- SIMILARITY: Belongs to the Dus family. Dus2 subfamily.
{ECO:0000305}.
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EMBL; AB101210; BAE07219.1; -; mRNA.
EMBL; AK000406; BAA91143.1; -; mRNA.
EMBL; AK290578; BAF83267.1; -; mRNA.
EMBL; AC130462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471092; EAW83207.1; -; Genomic_DNA.
EMBL; BC006527; AAH06527.1; -; mRNA.
CCDS; CCDS10859.1; -.
RefSeq; NP_001258691.1; NM_001271762.1.
RefSeq; NP_001258692.1; NM_001271763.1.
RefSeq; NP_060273.1; NM_017803.4.
UniGene; Hs.534460; -.
UniGene; Hs.744492; -.
PDB; 4WFS; X-ray; 2.68 A; A=14-333.
PDB; 4WFT; X-ray; 1.70 A; A/B/C=338-450.
PDB; 4XP7; X-ray; 1.90 A; A=1-340.
PDBsum; 4WFS; -.
PDBsum; 4WFT; -.
PDBsum; 4XP7; -.
ProteinModelPortal; Q9NX74; -.
SMR; Q9NX74; -.
BioGrid; 120261; 4.
IntAct; Q9NX74; 11.
MINT; Q9NX74; -.
STRING; 9606.ENSP00000351769; -.
ChEMBL; CHEMBL3879825; -.
iPTMnet; Q9NX74; -.
PhosphoSitePlus; Q9NX74; -.
DMDM; 73620832; -.
EPD; Q9NX74; -.
MaxQB; Q9NX74; -.
PaxDb; Q9NX74; -.
PeptideAtlas; Q9NX74; -.
PRIDE; Q9NX74; -.
ProteomicsDB; 83051; -.
DNASU; 54920; -.
Ensembl; ENST00000358896; ENSP00000351769; ENSG00000167264.
Ensembl; ENST00000565263; ENSP00000455229; ENSG00000167264.
GeneID; 54920; -.
KEGG; hsa:54920; -.
UCSC; uc002evi.5; human.
CTD; 54920; -.
DisGeNET; 54920; -.
EuPathDB; HostDB:ENSG00000167264.17; -.
GeneCards; DUS2; -.
HGNC; HGNC:26014; DUS2.
HPA; HPA042560; -.
HPA; HPA043528; -.
MIM; 609707; gene.
neXtProt; NX_Q9NX74; -.
OpenTargets; ENSG00000167264; -.
PharmGKB; PA142671937; -.
eggNOG; KOG2334; Eukaryota.
eggNOG; COG0042; LUCA.
GeneTree; ENSGT00550000075019; -.
HOGENOM; HOG000195580; -.
HOVERGEN; HBG079551; -.
InParanoid; Q9NX74; -.
KO; K05543; -.
OMA; TSGVIKM; -.
OrthoDB; EOG091G0CCW; -.
PhylomeDB; Q9NX74; -.
TreeFam; TF106151; -.
BRENDA; 1.3.1.91; 2681.
Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
GenomeRNAi; 54920; -.
PRO; PR:Q9NX74; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000167264; Expressed in 198 organ(s), highest expression level in amniotic fluid.
CleanEx; HS_DUS2L; -.
ExpressionAtlas; Q9NX74; baseline and differential.
Genevisible; Q9NX74; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0004860; F:protein kinase inhibitor activity; IDA:UniProtKB.
GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IBA:GO_Central.
GO; GO:0060548; P:negative regulation of cell death; IDA:UniProtKB.
CDD; cd00048; DSRM; 1.
CDD; cd02801; DUS_like_FMN; 1.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR035587; DUS-like_FMN-bd.
InterPro; IPR001269; tRNA_hU_synthase.
InterPro; IPR018517; tRNA_hU_synthase_CS.
PANTHER; PTHR11082; PTHR11082; 1.
Pfam; PF00035; dsrm; 1.
Pfam; PF01207; Dus; 1.
SMART; SM00358; DSRM; 1.
PROSITE; PS01136; UPF0034; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Endoplasmic reticulum;
Flavoprotein; FMN; Oxidoreductase; Phosphoprotein; Reference proteome;
RNA-binding; tRNA processing.
CHAIN 1 493 tRNA-dihydrouridine(20) synthase
[NAD(P)+]-like.
/FTId=PRO_0000162157.
DOMAIN 369 436 DRBM.
NP_BIND 18 20 FMN. {ECO:0000250|UniProtKB:Q5SMC7}.
NP_BIND 214 216 FMN. {ECO:0000250|UniProtKB:Q5SMC7}.
NP_BIND 242 243 FMN. {ECO:0000250|UniProtKB:Q5SMC7}.
ACT_SITE 116 116 Proton donor.
{ECO:0000250|UniProtKB:Q5SMC7}.
BINDING 87 87 FMN. {ECO:0000250|UniProtKB:Q5SMC7}.
BINDING 155 155 FMN. {ECO:0000250|UniProtKB:Q5SMC7}.
BINDING 183 183 FMN. {ECO:0000250|UniProtKB:Q5SMC7}.
MOD_RES 445 445 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 488 488 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
STRAND 14 16 {ECO:0000244|PDB:4XP7}.
TURN 20 23 {ECO:0000244|PDB:4XP7}.
HELIX 25 33 {ECO:0000244|PDB:4XP7}.
STRAND 37 40 {ECO:0000244|PDB:4XP7}.
HELIX 46 49 {ECO:0000244|PDB:4XP7}.
STRAND 53 57 {ECO:0000244|PDB:4XP7}.
TURN 58 61 {ECO:0000244|PDB:4XP7}.
STRAND 62 66 {ECO:0000244|PDB:4XP7}.
STRAND 72 76 {ECO:0000244|PDB:4XP7}.
HELIX 78 80 {ECO:0000244|PDB:4XP7}.
TURN 81 83 {ECO:0000244|PDB:4XP7}.
STRAND 84 89 {ECO:0000244|PDB:4XP7}.
HELIX 93 103 {ECO:0000244|PDB:4XP7}.
HELIX 104 106 {ECO:0000244|PDB:4XP7}.
STRAND 108 113 {ECO:0000244|PDB:4XP7}.
HELIX 130 132 {ECO:0000244|PDB:4XP7}.
HELIX 134 147 {ECO:0000244|PDB:4XP7}.
STRAND 152 158 {ECO:0000244|PDB:4XP7}.
HELIX 162 173 {ECO:0000244|PDB:4XP7}.
TURN 174 176 {ECO:0000244|PDB:4XP7}.
STRAND 178 186 {ECO:0000244|PDB:4XP7}.
HELIX 197 206 {ECO:0000244|PDB:4XP7}.
STRAND 211 214 {ECO:0000244|PDB:4XP7}.
TURN 218 220 {ECO:0000244|PDB:4XP7}.
STRAND 221 223 {ECO:0000244|PDB:4XP7}.
HELIX 224 234 {ECO:0000244|PDB:4XP7}.
STRAND 237 242 {ECO:0000244|PDB:4XP7}.
HELIX 243 247 {ECO:0000244|PDB:4XP7}.
HELIX 249 252 {ECO:0000244|PDB:4XP7}.
HELIX 260 273 {ECO:0000244|PDB:4XP7}.
HELIX 278 288 {ECO:0000244|PDB:4XP7}.
TURN 289 291 {ECO:0000244|PDB:4XP7}.
HELIX 296 303 {ECO:0000244|PDB:4XP7}.
HELIX 307 313 {ECO:0000244|PDB:4XP7}.
HELIX 317 333 {ECO:0000244|PDB:4XP7}.
HELIX 336 338 {ECO:0000244|PDB:4XP7}.
STRAND 351 355 {ECO:0000244|PDB:4WFT}.
HELIX 361 363 {ECO:0000244|PDB:4WFT}.
HELIX 370 380 {ECO:0000244|PDB:4WFT}.
STRAND 387 393 {ECO:0000244|PDB:4WFT}.
HELIX 394 396 {ECO:0000244|PDB:4WFT}.
STRAND 398 405 {ECO:0000244|PDB:4WFT}.
STRAND 408 414 {ECO:0000244|PDB:4WFT}.
STRAND 416 418 {ECO:0000244|PDB:4WFT}.
HELIX 419 433 {ECO:0000244|PDB:4WFT}.
SEQUENCE 493 AA; 55050 MW; 8CFE5046CCF79DCD CRC64;
MILNSLSLCY HNKLILAPMV RVGTLPMRLL ALDYGADIVY CEELIDLKMI QCKRVVNEVL
STVDFVAPDD RVVFRTCERE QNRVVFQMGT SDAERALAVA RLVENDVAGI DVNMGCPKQY
STKGGMGAAL LSDPDKIEKI LSTLVKGTRR PVTCKIRILP SLEDTLSLVK RIERTGIAAI
AVHGRKREER PQHPVSCEVI KAIADTLSIP VIANGGSHDH IQQYSDIEDF RQATAASSVM
VARAAMWNPS IFLKEGLRPL EEVMQKYIRY AVQYDNHYTN TKYCLCQMLR EQLESPQGRL
LHAAQSSREI CEAFGLGAFY EETTQELDAQ QARLSAKTSE QTGEPAEDTS GVIKMAVKFD
RRAYPAQITP KMCLLEWCRR EKLAQPVYET VQRPLDRLFS SIVTVAEQKY QSTLWDKSKK
LAEQAAAIVC LRSQGLPEGR LGEESPSLHK RKREAPDQDP GGPRAQELAQ PGDLCKKPFV
ALGSGEESPL EGW


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