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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
 
 
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