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Q9NX74

- DUS2L_HUMAN

UniProt

Q9NX74 - DUS2L_HUMAN

Protein

tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

Gene

DUS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Cofactori

    FAD.By similarity

    GO - Molecular functioni

    1. double-stranded RNA binding Source: UniProtKB
    2. flavin adenine dinucleotide binding Source: InterPro
    3. protein binding Source: UniProtKB
    4. protein kinase inhibitor activity Source: UniProtKB
    5. tRNA dihydrouridine synthase activity Source: InterPro

    GO - Biological processi

    1. negative regulation of cell death Source: UniProtKB
    2. negative regulation of protein kinase activity Source: GOC

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    FAD, Flavoprotein, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (EC:1.3.1.-)
    Alternative name(s):
    Dihydrouridine synthase 2
    Up-regulated in lung cancer protein 8
    Short name:
    URLC8
    tRNA-dihydrouridine synthase 2-like
    Short name:
    hDUS2
    Gene namesi
    Name:DUS2
    Synonyms:DUS2L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:26014. DUS2.

    Subcellular locationi

    Cytoplasm 1 Publication. Endoplasmic reticulum 1 Publication
    Note: Mainly at the endoplasmic reticulum.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. endoplasmic reticulum Source: UniProtKB-SubCell
    3. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671937.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 493493tRNA-dihydrouridine(20) synthase [NAD(P)+]-likePRO_0000162157Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei488 – 4881Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NX74.
    PaxDbiQ9NX74.
    PRIDEiQ9NX74.

    PTM databases

    PhosphoSiteiQ9NX74.

    Expressioni

    Tissue specificityi

    Weak expression in heart, placenta and skeletal muscle. Up-regulated in most lung cancer cells (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ9NX74.
    BgeeiQ9NX74.
    CleanExiHS_DUS2L.
    GenevestigatoriQ9NX74.

    Organism-specific databases

    HPAiHPA042560.
    HPA043528.

    Interactioni

    Subunit structurei

    Interacts with EPRS. Interacts (via DRBM domain) with PRKRA and EIF2AK2/PKR (via DRBM 1 domain).2 Publications

    Protein-protein interaction databases

    BioGridi120261. 4 interactions.
    IntActiQ9NX74. 3 interactions.
    MINTiMINT-3076069.
    STRINGi9606.ENSP00000351769.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NX74.
    SMRiQ9NX74. Positions 13-270, 352-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini369 – 43668DRBMAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Dus family. Dus2 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0042.
    HOGENOMiHOG000195580.
    HOVERGENiHBG079551.
    InParanoidiQ9NX74.
    KOiK05543.
    OMAiEDTSGVI.
    PhylomeDBiQ9NX74.
    TreeFamiTF106151.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    3.30.160.20. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR014720. dsRNA-bd_dom.
    IPR001269. tRNA_hU_synthase.
    IPR018517. tRNA_hU_synthase_CS.
    [Graphical view]
    PANTHERiPTHR11082. PTHR11082. 1 hit.
    PfamiPF00035. dsrm. 1 hit.
    PF01207. Dus. 1 hit.
    [Graphical view]
    SMARTiSM00358. DSRM. 1 hit.
    [Graphical view]
    PROSITEiPS01136. UPF0034. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9NX74-1 [UniParc]FASTAAdd to Basket

    « Hide

    MILNSLSLCY HNKLILAPMV RVGTLPMRLL ALDYGADIVY CEELIDLKMI    50
    QCKRVVNEVL STVDFVAPDD RVVFRTCERE QNRVVFQMGT SDAERALAVA 100
    RLVENDVAGI DVNMGCPKQY STKGGMGAAL LSDPDKIEKI LSTLVKGTRR 150
    PVTCKIRILP SLEDTLSLVK RIERTGIAAI AVHGRKREER PQHPVSCEVI 200
    KAIADTLSIP VIANGGSHDH IQQYSDIEDF RQATAASSVM VARAAMWNPS 250
    IFLKEGLRPL EEVMQKYIRY AVQYDNHYTN TKYCLCQMLR EQLESPQGRL 300
    LHAAQSSREI CEAFGLGAFY EETTQELDAQ QARLSAKTSE QTGEPAEDTS 350
    GVIKMAVKFD RRAYPAQITP KMCLLEWCRR EKLAQPVYET VQRPLDRLFS 400
    SIVTVAEQKY QSTLWDKSKK LAEQAAAIVC LRSQGLPEGR LGEESPSLHK 450
    RKREAPDQDP GGPRAQELAQ PGDLCKKPFV ALGSGEESPL EGW 493
    Length:493
    Mass (Da):55,050
    Last modified:October 1, 2000 - v1
    Checksum:i8CFE5046CCF79DCD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB101210 mRNA. Translation: BAE07219.1.
    AK000406 mRNA. Translation: BAA91143.1.
    AK290578 mRNA. Translation: BAF83267.1.
    AC130462 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83207.1.
    BC006527 mRNA. Translation: AAH06527.1.
    CCDSiCCDS10859.1.
    RefSeqiNP_001258691.1. NM_001271762.1.
    NP_001258692.1. NM_001271763.1.
    NP_060273.1. NM_017803.4.
    UniGeneiHs.534460.
    Hs.744492.

    Genome annotation databases

    EnsembliENST00000358896; ENSP00000351769; ENSG00000167264.
    ENST00000565263; ENSP00000455229; ENSG00000167264.
    GeneIDi54920.
    KEGGihsa:54920.
    UCSCiuc002evi.4. human.

    Polymorphism databases

    DMDMi73620832.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB101210 mRNA. Translation: BAE07219.1 .
    AK000406 mRNA. Translation: BAA91143.1 .
    AK290578 mRNA. Translation: BAF83267.1 .
    AC130462 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83207.1 .
    BC006527 mRNA. Translation: AAH06527.1 .
    CCDSi CCDS10859.1.
    RefSeqi NP_001258691.1. NM_001271762.1.
    NP_001258692.1. NM_001271763.1.
    NP_060273.1. NM_017803.4.
    UniGenei Hs.534460.
    Hs.744492.

    3D structure databases

    ProteinModelPortali Q9NX74.
    SMRi Q9NX74. Positions 13-270, 352-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120261. 4 interactions.
    IntActi Q9NX74. 3 interactions.
    MINTi MINT-3076069.
    STRINGi 9606.ENSP00000351769.

    PTM databases

    PhosphoSitei Q9NX74.

    Polymorphism databases

    DMDMi 73620832.

    Proteomic databases

    MaxQBi Q9NX74.
    PaxDbi Q9NX74.
    PRIDEi Q9NX74.

    Protocols and materials databases

    DNASUi 54920.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358896 ; ENSP00000351769 ; ENSG00000167264 .
    ENST00000565263 ; ENSP00000455229 ; ENSG00000167264 .
    GeneIDi 54920.
    KEGGi hsa:54920.
    UCSCi uc002evi.4. human.

    Organism-specific databases

    CTDi 54920.
    GeneCardsi GC16P068021.
    HGNCi HGNC:26014. DUS2.
    HPAi HPA042560.
    HPA043528.
    MIMi 609707. gene.
    neXtProti NX_Q9NX74.
    PharmGKBi PA142671937.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0042.
    HOGENOMi HOG000195580.
    HOVERGENi HBG079551.
    InParanoidi Q9NX74.
    KOi K05543.
    OMAi EDTSGVI.
    PhylomeDBi Q9NX74.
    TreeFami TF106151.

    Miscellaneous databases

    GenomeRNAii 54920.
    NextBioi 57992.
    PROi Q9NX74.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NX74.
    Bgeei Q9NX74.
    CleanExi HS_DUS2L.
    Genevestigatori Q9NX74.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    3.30.160.20. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR014720. dsRNA-bd_dom.
    IPR001269. tRNA_hU_synthase.
    IPR018517. tRNA_hU_synthase_CS.
    [Graphical view ]
    PANTHERi PTHR11082. PTHR11082. 1 hit.
    Pfami PF00035. dsrm. 1 hit.
    PF01207. Dus. 1 hit.
    [Graphical view ]
    SMARTi SM00358. DSRM. 1 hit.
    [Graphical view ]
    PROSITEi PS01136. UPF0034. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis."
      Kato T., Daigo Y., Hayama S., Ishikawa N., Yamabuki T., Ito T., Miyamoto M., Kondo S., Nakamura Y.
      Cancer Res. 65:5638-5646(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH EPRS.
    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: Gastric carcinoma.
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      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.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Colon.
    6. "Interaction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKR."
      Mittelstadt M., Frump A., Khuu T., Fowlkes V., Handy I., Patel C.V., Patel R.C.
      Nucleic Acids Res. 36:998-1008(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PRKRA AND EIF2AK2.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDUS2L_HUMAN
    AccessioniPrimary (citable) accession number: Q9NX74
    Secondary accession number(s): A8K3G3, Q4H4D9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 106 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3