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Q9DBN9

- DDX59_MOUSE

UniProt

Q9DBN9 - DDX59_MOUSE

Protein

Probable ATP-dependent RNA helicase DDX59

Gene

Ddx59

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri104 – 13330HIT-typeAdd
    BLAST
    Nucleotide bindingi247 – 2548ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. helicase activity Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. RNA binding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable ATP-dependent RNA helicase DDX59 (EC:3.6.4.13)
    Alternative name(s):
    DEAD box protein 59
    Gene namesi
    Name:Ddx59
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1915247. Ddx59.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 619619Probable ATP-dependent RNA helicase DDX59PRO_0000282714Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei64 – 641PhosphoserineBy similarity
    Modified residuei160 – 1601PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9DBN9.
    PRIDEiQ9DBN9.

    PTM databases

    PhosphoSiteiQ9DBN9.

    Expressioni

    Developmental stagei

    AT 11.5 dpc, expressed in the developing snout region, eye and limb buds. At 13.5 dpc, highly enriched in the lips, palatal shelves (secondary palate), and developing limb buds.1 Publication

    Gene expression databases

    BgeeiQ9DBN9.
    CleanExiMM_DDX59.
    GenevestigatoriQ9DBN9.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DBN9.
    SMRiQ9DBN9. Positions 96-143, 168-583.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini234 – 405172Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini416 – 579164Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi203 – 23129Q motifAdd
    BLAST
    Motifi353 – 3564DEAD box

    Domaini

    The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 HIT-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri104 – 13330HIT-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0513.
    GeneTreeiENSGT00740000115519.
    HOGENOMiHOG000006599.
    HOVERGENiHBG106120.
    InParanoidiQ9DBN9.
    OMAiEHPFILN.
    OrthoDBiEOG7B8S3D.
    PhylomeDBiQ9DBN9.
    TreeFamiTF330866.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    IPR007529. Znf_HIT.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF04438. zf-HIT. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9DBN9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MFVPRSLKIK RSSNDDLKSG EAKKSKPEAG GLQVEGDRDT PVHTSVTEEA    50
    VTADKPGHAS STNSPSCQLA EVSSTGPDEG VKDSHPSEEP VKSFSKTQRW 100
    PEPGEPVCVV CGRYGEYICD KTDEDVCSLE CKAKHLLQVK EGEGSLRPSS 150
    PQRVAAEPES PLDAFYVYKE HPFIVTLKED QIETLKQQLG ISVQGQDVAR 200
    PIIDFEHCGF PETLNQNLKK SGYEVPTPIQ MQMIPVGLLG RDILASADTG 250
    SGKTAAFLLP VIIRAFSEDK TPSALILTPT RELAIQIERQ AKELMSGLPR 300
    MKTVLLVGGL PLPPQLYRLR QHVKVIIATP GRLLDIIKQS SVSLSGIKIV 350
    VVDEADTMLK MGFQQQVLDV LEHTPGDCQT ILVSATIPDS IEQLTDQLLH 400
    NPVRIITGDK NLPCASVRQI ILWVEDPAKK KKLFEILNDQ KLFKPPVLVF 450
    VDCKLGADLL SEAVQKITGL NSTSIHSEKS QVERRDILKG LLEGDYEVVV 500
    STGVLGRGLD LVNVKLVVNF DMPSSMDEYV HQVGRVGRLG QNGTAITFIN 550
    NNSKRLFWDV AKRVKPTGSI LPPQLLNSPY LHEQKRKEQQ KDRQTQNSLV 600
    TGANLMDIIR KHEKSSSQK 619
    Length:619
    Mass (Da):68,234
    Last modified:June 1, 2001 - v1
    Checksum:iE4FE6E723D125697
    GO
    Isoform 2 (identifier: Q9DBN9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         269-292: DKTPSALILTPTRELAIQIERQAK → VIYQSDMSSSLKQTRDLPSFIVCN
         293-619: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:292
    Mass (Da):31,851
    Checksum:iB178BF6B8DCA3B90
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti208 – 2081C → S in BAB28694. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei269 – 29224DKTPS…ERQAK → VIYQSDMSSSLKQTRDLPSF IVCN in isoform 2. 1 PublicationVSP_026429Add
    BLAST
    Alternative sequencei293 – 619327Missing in isoform 2. 1 PublicationVSP_026430Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004833 mRNA. Translation: BAB23601.1.
    AK013179 mRNA. Translation: BAB28694.1.
    AK076462 mRNA. Translation: BAC36354.1.
    BC023840 mRNA. Translation: AAH23840.1.
    CCDSiCCDS15326.1. [Q9DBN9-1]
    RefSeqiNP_080776.1. NM_026500.3. [Q9DBN9-1]
    UniGeneiMm.385462.
    Mm.486546.

    Genome annotation databases

    EnsembliENSMUST00000027655; ENSMUSP00000027655; ENSMUSG00000026404. [Q9DBN9-1]
    GeneIDi67997.
    KEGGimmu:67997.
    UCSCiuc007cut.1. mouse. [Q9DBN9-2]
    uc007cuu.2. mouse. [Q9DBN9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004833 mRNA. Translation: BAB23601.1 .
    AK013179 mRNA. Translation: BAB28694.1 .
    AK076462 mRNA. Translation: BAC36354.1 .
    BC023840 mRNA. Translation: AAH23840.1 .
    CCDSi CCDS15326.1. [Q9DBN9-1 ]
    RefSeqi NP_080776.1. NM_026500.3. [Q9DBN9-1 ]
    UniGenei Mm.385462.
    Mm.486546.

    3D structure databases

    ProteinModelPortali Q9DBN9.
    SMRi Q9DBN9. Positions 96-143, 168-583.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9DBN9.

    Proteomic databases

    MaxQBi Q9DBN9.
    PRIDEi Q9DBN9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027655 ; ENSMUSP00000027655 ; ENSMUSG00000026404 . [Q9DBN9-1 ]
    GeneIDi 67997.
    KEGGi mmu:67997.
    UCSCi uc007cut.1. mouse. [Q9DBN9-2 ]
    uc007cuu.2. mouse. [Q9DBN9-1 ]

    Organism-specific databases

    CTDi 83479.
    MGIi MGI:1915247. Ddx59.

    Phylogenomic databases

    eggNOGi COG0513.
    GeneTreei ENSGT00740000115519.
    HOGENOMi HOG000006599.
    HOVERGENi HBG106120.
    InParanoidi Q9DBN9.
    OMAi EHPFILN.
    OrthoDBi EOG7B8S3D.
    PhylomeDBi Q9DBN9.
    TreeFami TF330866.

    Miscellaneous databases

    ChiTaRSi DDX59. mouse.
    NextBioi 326168.
    PROi Q9DBN9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9DBN9.
    CleanExi MM_DDX59.
    Genevestigatori Q9DBN9.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    IPR007529. Znf_HIT.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF04438. zf-HIT. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Head and Lung.
    2. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    3. "Mutations in DDX59 implicate RNA helicase in the pathogenesis of orofaciodigital syndrome."
      Shamseldin H.E., Rajab A., Alhashem A., Shaheen R., Al-Shidi T., Alamro R., Al Harassi S., Alkuraya F.S.
      Am. J. Hum. Genet. 93:555-560(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiDDX59_MOUSE
    AccessioniPrimary (citable) accession number: Q9DBN9
    Secondary accession number(s): Q8C667, Q9CSD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3