DUS1L_HUMAN
ID DUS1L_HUMAN Reviewed; 473 AA.
AC Q6P1R4; A6NHV4; Q96AI3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like;
DE EC=1.3.1.88 {ECO:0000305|PubMed:34798057};
DE AltName: Full=tRNA-dihydrouridine synthase 1-like;
GN Name=DUS1L;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Colon, and Pancreas;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=34798057; DOI=10.1016/j.molcel.2021.11.003;
RA Finet O., Yague-Sanz C., Krueger L.K., Tran P., Migeot V., Louski M.,
RA Nevers A., Rougemaille M., Sun J., Ernst F.G.M., Wacheul L., Wery M.,
RA Morillon A., Dedon P., Lafontaine D.L.J., Hermand D.;
RT "Transcription-wide mapping of dihydrouridine reveals that mRNA
RT dihydrouridylation is required for meiotic chromosome segregation.";
RL Mol. Cell 0:0-0(2021).
CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base
CC found in the D-loop of most tRNAs. {ECO:0000269|PubMed:34798057}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(16) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(16) in tRNA; Xref=Rhea:RHEA:53376, Rhea:RHEA-COMP:13543,
CC Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000305|PubMed:34798057};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53378;
CC Evidence={ECO:0000305|PubMed:34798057};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(16) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(16) in tRNA; Xref=Rhea:RHEA:53380, Rhea:RHEA-COMP:13543,
CC Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000305|PubMed:34798057};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53382;
CC Evidence={ECO:0000305|PubMed:34798057};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(17) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(17) in tRNA; Xref=Rhea:RHEA:53372, Rhea:RHEA-COMP:13541,
CC Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000250|UniProtKB:P53759};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53374;
CC Evidence={ECO:0000250|UniProtKB:P53759};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(17) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(17) in tRNA; Xref=Rhea:RHEA:53368, Rhea:RHEA-COMP:13541,
CC Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000250|UniProtKB:P53759};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53370;
CC Evidence={ECO:0000250|UniProtKB:P53759};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q5SMC7};
CC -!- INTERACTION:
CC Q6P1R4; Q13554-3: CAMK2B; NbExp=3; IntAct=EBI-6660325, EBI-11523526;
CC Q6P1R4; Q13555-5: CAMK2G; NbExp=3; IntAct=EBI-6660325, EBI-12020154;
CC Q6P1R4; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-6660325, EBI-16439278;
CC -!- SIMILARITY: Belongs to the Dus family. Dus1 subfamily. {ECO:0000305}.
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DR EMBL; AC135056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017081; AAH17081.4; -; mRNA.
DR EMBL; BC062566; AAH62566.1; -; mRNA.
DR EMBL; BC064918; AAH64918.1; -; mRNA.
DR CCDS; CCDS32775.1; -.
DR RefSeq; NP_071439.3; NM_022156.4.
DR AlphaFoldDB; Q6P1R4; -.
DR SMR; Q6P1R4; -.
DR BioGRID; 122073; 9.
DR IntAct; Q6P1R4; 6.
DR STRING; 9606.ENSP00000346280; -.
DR iPTMnet; Q6P1R4; -.
DR PhosphoSitePlus; Q6P1R4; -.
DR BioMuta; DUS1L; -.
DR DMDM; 74749069; -.
DR EPD; Q6P1R4; -.
DR jPOST; Q6P1R4; -.
DR MassIVE; Q6P1R4; -.
DR MaxQB; Q6P1R4; -.
DR PaxDb; Q6P1R4; -.
DR PeptideAtlas; Q6P1R4; -.
DR PRIDE; Q6P1R4; -.
DR ProteomicsDB; 66872; -.
DR Antibodypedia; 19877; 124 antibodies from 23 providers.
DR DNASU; 64118; -.
DR Ensembl; ENST00000306796.10; ENSP00000303515.5; ENSG00000169718.18.
DR Ensembl; ENST00000354321.11; ENSP00000346280.7; ENSG00000169718.18.
DR GeneID; 64118; -.
DR KEGG; hsa:64118; -.
DR MANE-Select; ENST00000306796.10; ENSP00000303515.5; NM_022156.5; NP_071439.3.
DR UCSC; uc002kdq.5; human.
DR CTD; 64118; -.
DR DisGeNET; 64118; -.
DR GeneCards; DUS1L; -.
DR HGNC; HGNC:30086; DUS1L.
DR HPA; ENSG00000169718; Low tissue specificity.
DR neXtProt; NX_Q6P1R4; -.
DR OpenTargets; ENSG00000169718; -.
DR PharmGKB; PA142671936; -.
DR VEuPathDB; HostDB:ENSG00000169718; -.
DR eggNOG; KOG2335; Eukaryota.
DR GeneTree; ENSGT00550000075089; -.
DR HOGENOM; CLU_013299_5_1_1; -.
DR InParanoid; Q6P1R4; -.
DR OMA; VKQYPPC; -.
DR OrthoDB; 1318230at2759; -.
DR PhylomeDB; Q6P1R4; -.
DR TreeFam; TF313398; -.
DR PathwayCommons; Q6P1R4; -.
DR SignaLink; Q6P1R4; -.
DR BioGRID-ORCS; 64118; 20 hits in 1080 CRISPR screens.
DR ChiTaRS; DUS1L; human.
DR GenomeRNAi; 64118; -.
DR Pharos; Q6P1R4; Tbio.
DR PRO; PR:Q6P1R4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6P1R4; protein.
DR Bgee; ENSG00000169718; Expressed in lower esophagus mucosa and 187 other tissues.
DR ExpressionAtlas; Q6P1R4; baseline and differential.
DR Genevisible; Q6P1R4; HS.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IBA:GO_Central.
DR GO; GO:0002943; P:tRNA dihydrouridine synthesis; IDA:UniProtKB.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR Pfam; PF01207; Dus; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; NAD; NADP; Oxidoreductase; Reference proteome;
KW tRNA processing.
FT CHAIN 1..473
FT /note="tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-
FT like"
FT /id="PRO_0000247226"
FT REGION 339..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 23..25
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 79
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 147
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 175
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 208..210
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 232..233
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
SQ SEQUENCE 473 AA; 53230 MW; 9765C2BD7B0C6157 CRC64;
MPKLQGFEFW SRTLRGARHV VAPMVDQSEL AWRLLSRRHG AQLCYTPMLH AQVFVRDANY
RKENLYCEVC PEDRPLIVQF CANDPEVFVQ AALLAQDYCD AIDLNLGCPQ MIAKRGHYGA
FLQDEWDLLQ RMILLAHEKL SVPVTCKIRV FPEIDKTVRY AQMLEKAGCQ LLTVHGRTKE
QKGPLSGAAS WEHIKAVRKA VAIPVFANGN IQCLQDVERC LRDTGVQGVM SAEGNLHNPA
LFEGRSPAVW ELAEEYLDIV REHPCPLSYV RAHLFKLWHH TLQVHQELRE ELAKVKTLEG
IAAVSQELKL RCQEEISRQE GAKPTGDLPF HWICQPYIRP GPREGSKEKA GARSKRALEE
EEGGTEVLSK NKQKKQLRNP HKTFDPSLKP KYAKCDQCGN PKGNRCVFSL CRGCCKKRAS
KETADCPGHG LLFKTKLEKS LAWKEAQPEL QEPQPAAPGT PGGFSEVMGS ALA
