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P54823

- DDX6_MOUSE

UniProt

P54823 - DDX6_MOUSE

Protein

Probable ATP-dependent RNA helicase DDX6

Gene

Ddx6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    In the process of mRNA degradation, may play a role in mRNA decapping.

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi140 – 1478ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent helicase activity Source: InterPro
    3. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. cytoplasmic mRNA processing body assembly Source: MGI

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable ATP-dependent RNA helicase DDX6 (EC:3.6.4.13)
    Alternative name(s):
    ATP-dependent RNA helicase p54
    DEAD box protein 6
    Oncogene RCK homolog
    Gene namesi
    Name:Ddx6
    Synonyms:Hlr2, Rck
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:104976. Ddx6.

    Subcellular locationi

    CytoplasmP-body By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytoplasmic mRNA processing body Source: MGI
    3. cytoplasmic stress granule Source: Ensembl
    4. RISC complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 483483Probable ATP-dependent RNA helicase DDX6PRO_0000054984Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei36 – 361PhosphothreonineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP54823.
    PaxDbiP54823.
    PRIDEiP54823.

    PTM databases

    PhosphoSiteiP54823.

    Expressioni

    Developmental stagei

    Abundant expression in growing oocytes, levels decline in primary and secondary oocytes, and degradation appears to be complete by the mid-late two-cell stage.1 Publication

    Gene expression databases

    BgeeiP54823.
    CleanExiMM_DDX6.
    GenevestigatoriP54823.

    Interactioni

    Subunit structurei

    Forms a complex with DCP1A, DCP2, EDC3 and EDC4/HEDLS By similarity. Interacts with LIMD1, WTIP and AJUBA By similarity. Interacts with APOBEC3G in an RNA-dependent manner By similarity. Interacts with RC3H1.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi199087. 2 interactions.
    IntActiP54823. 5 interactions.
    MINTiMINT-4093002.

    Structurei

    3D structure databases

    ProteinModelPortaliP54823.
    SMRiP54823. Positions 94-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini127 – 298172Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini308 – 468161Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi96 – 12429Q motifAdd
    BLAST
    Motifi246 – 2494DEAD box

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0513.
    GeneTreeiENSGT00740000115573.
    HOGENOMiHOG000268797.
    HOVERGENiHBG106685.
    InParanoidiP54823.
    KOiK12614.
    OMAiLLQFHPK.
    OrthoDBiEOG7D85W7.
    PhylomeDBiP54823.
    TreeFamiTF300440.

    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.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P54823-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTARTENPV IMGLSSQNGQ LRGPVKASAG PGGGGTQPQP QLNQLKNTST    50
    INNGTPQQAQ SMAATIKPGD DWKKTLKLPP KDLRIKTSDV TSTKGNEFED 100
    YCLKRELLMG IFEMGWEKPS PIQEESIPIA LSGRDILARA KNGTGKSGAY 150
    LIPLLERLDL KKDNIQAMVI VPTRELALQV SQICIQVSKH MGGAKVMATT 200
    GGTNLRDDIM RLDDTVHVVI ATPGRILDLI KKGVAKVDHV QMIVLDEADK 250
    LLSQDFVQIM EDIILTLPKN RQILLYSATF PLSVQKFMNS HLQKPYEINL 300
    MEELTLKGVT QYYAYVTERQ KVHCLNTLFS RLQINQSIIF CNSSQRVELL 350
    AKKISQLGYS CFYIHAKMRQ EHRNRVFHDF RNGLCRNLVC TDLFTRGIDI 400
    QAVNVVINFD FPKLAETYLH RIGRSGRFGH LGLAINLITY DDRFNLKSIE 450
    EQLGTEIKPI PSNIDKSLYV AEYHSEPAED EKP 483
    Length:483
    Mass (Da):54,192
    Last modified:October 1, 1996 - v1
    Checksum:i9AD22D171F8BC14D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 425PQPQL → TQQQM in AAB94769. (PubMed:9883581)Curated
    Sequence conflicti202 – 2021G → P in AAB94769. (PubMed:9883581)Curated
    Sequence conflicti241 – 2411Q → R in BAC35670. (PubMed:15489334)Curated
    Sequence conflicti311 – 3111Q → E in BAC35670. (PubMed:15489334)Curated
    Sequence conflicti381 – 3811R → E in AAB94769. (PubMed:9883581)Curated
    Sequence conflicti407 – 4071I → M in BAC35670. (PubMed:15489334)Curated
    Sequence conflicti422 – 4221I → V in AAB94769. (PubMed:9883581)Curated
    Sequence conflicti478 – 4781A → V in AAB94769. (PubMed:9883581)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50494 mRNA. Translation: BAA09088.1.
    AK054144 mRNA. Translation: BAC35670.1.
    AK148483 mRNA. Translation: BAE28578.1.
    BC021452 mRNA. Translation: AAH21452.1.
    AF038995 mRNA. Translation: AAB94769.1.
    CCDSiCCDS23116.1.
    RefSeqiNP_001104296.1. NM_001110826.1.
    NP_031867.1. NM_007841.4.
    NP_851841.2. NM_181324.3.
    UniGeneiMm.267061.

    Genome annotation databases

    EnsembliENSMUST00000170489; ENSMUSP00000128421; ENSMUSG00000032097.
    GeneIDi13209.
    KEGGimmu:13209.
    UCSCiuc009pdy.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50494 mRNA. Translation: BAA09088.1 .
    AK054144 mRNA. Translation: BAC35670.1 .
    AK148483 mRNA. Translation: BAE28578.1 .
    BC021452 mRNA. Translation: AAH21452.1 .
    AF038995 mRNA. Translation: AAB94769.1 .
    CCDSi CCDS23116.1.
    RefSeqi NP_001104296.1. NM_001110826.1.
    NP_031867.1. NM_007841.4.
    NP_851841.2. NM_181324.3.
    UniGenei Mm.267061.

    3D structure databases

    ProteinModelPortali P54823.
    SMRi P54823. Positions 94-472.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199087. 2 interactions.
    IntActi P54823. 5 interactions.
    MINTi MINT-4093002.

    PTM databases

    PhosphoSitei P54823.

    Proteomic databases

    MaxQBi P54823.
    PaxDbi P54823.
    PRIDEi P54823.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000170489 ; ENSMUSP00000128421 ; ENSMUSG00000032097 .
    GeneIDi 13209.
    KEGGi mmu:13209.
    UCSCi uc009pdy.2. mouse.

    Organism-specific databases

    CTDi 1656.
    MGIi MGI:104976. Ddx6.

    Phylogenomic databases

    eggNOGi COG0513.
    GeneTreei ENSGT00740000115573.
    HOGENOMi HOG000268797.
    HOVERGENi HBG106685.
    InParanoidi P54823.
    KOi K12614.
    OMAi LLQFHPK.
    OrthoDBi EOG7D85W7.
    PhylomeDBi P54823.
    TreeFami TF300440.

    Miscellaneous databases

    NextBioi 283376.
    PROi P54823.
    SOURCEi Search...

    Gene expression databases

    Bgeei P54823.
    CleanExi MM_DDX6.
    Genevestigatori P54823.

    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.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of a murine cDNA homologous to the human RCK/P54, a lymphoma-linked chromosomal translocation junction gene on 11q23."
      Seto M., Yamamoto K., Takahashi T., Ueda R.
      Gene 166:293-296(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Spleen.
    2. "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].
      Strain: C57BL/6J.
      Tissue: Oviduct and Pancreas.
    3. "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: Kidney.
    4. "RNA-binding proteins in mouse oocytes and embryos: expression of genes encoding Y box, DEAD box RNA helicase, and polyA binding proteins."
      Paynton B.V.
      Dev. Genet. 23:285-298(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-478, DEVELOPMENTAL STAGE.
      Strain: CB6F1/J.
      Tissue: Oocyte.
    5. "Roquin binds inducible costimulator mRNA and effectors of mRNA decay to induce microRNA-independent post-transcriptional repression."
      Glasmacher E., Hoefig K.P., Vogel K.U., Rath N., Du L., Wolf C., Kremmer E., Wang X., Heissmeyer V.
      Nat. Immunol. 11:725-733(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RC3H1.

    Entry informationi

    Entry nameiDDX6_MOUSE
    AccessioniPrimary (citable) accession number: P54823
    Secondary accession number(s): O54979, Q3UFI3, Q8BW68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 121 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