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Q9H0S4

- DDX47_HUMAN

UniProt

Q9H0S4 - DDX47_HUMAN

Protein

Probable ATP-dependent RNA helicase DDX47

Gene

DDX47

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Involved in apoptosis. May have a role in rRNA processing and mRNA splicing. Associates with pre-rRNA precursors.2 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi68 – 758ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent helicase activity Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. extrinsic apoptotic signaling pathway via death domain receptors Source: UniProtKB
    2. mRNA processing Source: UniProtKB-KW
    3. RNA splicing Source: UniProtKB
    4. rRNA processing Source: UniProtKB

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Apoptosis, mRNA processing, mRNA splicing, rRNA processing

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable ATP-dependent RNA helicase DDX47 (EC:3.6.4.13)
    Alternative name(s):
    DEAD box protein 47
    Gene namesi
    Name:DDX47
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:18682. DDX47.

    Subcellular locationi

    Nucleusnucleolus 2 Publications
    Note: Localizes in the nucleolar-organizing region during ribosome biogenesis.

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. nucleolus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134918403.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 455454Probable ATP-dependent RNA helicase DDX47PRO_0000055050Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei9 – 91Phosphoserine1 Publication
    Modified residuei424 – 4241Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H0S4.
    PaxDbiQ9H0S4.
    PRIDEiQ9H0S4.

    2D gel databases

    SWISS-2DPAGEQ9H0S4.

    PTM databases

    PhosphoSiteiQ9H0S4.

    Expressioni

    Gene expression databases

    BgeeiQ9H0S4.
    CleanExiHS_DDX47.
    GenevestigatoriQ9H0S4.

    Organism-specific databases

    HPAiHPA014855.

    Interactioni

    Subunit structurei

    Interacts with AGO1 and AGO2. Interacts with GABARAP. Interacts with NOL8; the interaction is RNA-dependent.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GABARAPO951663EBI-2515241,EBI-712001

    Protein-protein interaction databases

    BioGridi119375. 18 interactions.
    IntActiQ9H0S4. 13 interactions.
    MINTiMINT-3056694.
    STRINGi9606.ENSP00000350698.

    Structurei

    Secondary structure

    1
    455
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 236
    Helixi27 – 293
    Helixi33 – 419
    Helixi49 – 5911
    Beta strandi64 – 674
    Helixi74 – 8815
    Beta strandi95 – 984
    Helixi102 – 11615
    Helixi117 – 1193
    Beta strandi123 – 1264
    Helixi132 – 1409
    Beta strandi144 – 1485
    Helixi150 – 15910
    Beta strandi170 – 1734
    Helixi176 – 1816
    Helixi185 – 1939
    Beta strandi197 – 20711
    Helixi210 – 21910
    Beta strandi224 – 2274

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BERX-ray1.40A5-230[»]
    ProteinModelPortaliQ9H0S4.
    SMRiQ9H0S4. Positions 11-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H0S4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 226172Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini237 – 397161Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi24 – 5229Q motifAdd
    BLAST
    Motifi174 – 1774DEAD box

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0513.
    HOGENOMiHOG000268802.
    HOVERGENiHBG100512.
    InParanoidiQ9H0S4.
    KOiK14777.
    OMAiNKFRAGS.
    OrthoDBiEOG7GTT3T.
    PhylomeDBiQ9H0S4.
    TreeFamiTF105714.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H0S4-1) [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

    MAAPEEHDSP TEASQPIVEE EETKTFKDLG VTDVLCEACD QLGWTKPTKI    50
    QIEAIPLALQ GRDIIGLAET GSGKTGAFAL PILNALLETP QRLFALVLTP 100
    TRELAFQISE QFEALGSSIG VQSAVIVGGI DSMSQSLALA KKPHIIIATP 150
    GRLIDHLENT KGFNLRALKY LVMDEADRIL NMDFETEVDK ILKVIPRDRK 200
    TFLFSATMTK KVQKLQRAAL KNPVKCAVSS KYQTVEKLQQ YYIFIPSKFK 250
    DTYLVYILNE LAGNSFMIFC STCNNTQRTA LLLRNLGFTA IPLHGQMSQS 300
    KRLGSLNKFK AKARSILLAT DVASRGLDIP HVDVVVNFDI PTHSKDYIHR 350
    VGRTARAGRS GKAITFVTQY DVELFQRIEH LIGKKLPGFP TQDDEVMMLT 400
    ERVAEAQRFA RMELREHGEK KKRSREDAGD NDDTEGAIGV RNKVAGGKMK 450
    KRKGR 455
    Length:455
    Mass (Da):50,647
    Last modified:March 1, 2001 - v1
    Checksum:i5F64F26AD2C11286
    GO
    Isoform 2 (identifier: Q9H0S4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         251-299: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:406
    Mass (Da):45,169
    Checksum:iE6FFADA03AFAB679
    GO

    Sequence cautioni

    The sequence AAF23354.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551I → V in BAB70762. (PubMed:16541075)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei251 – 29949Missing in isoform 2. 1 PublicationVSP_045239Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136666 mRNA. Translation: CAB66601.1.
    AK054574 mRNA. Translation: BAB70762.1.
    AK127712 mRNA. Translation: BAG54556.1.
    AC007215 Genomic DNA. No translation available.
    CH471094 Genomic DNA. Translation: EAW96277.1.
    CH471094 Genomic DNA. Translation: EAW96283.1.
    BC009379 mRNA. Translation: AAH09379.2.
    BC068009 mRNA. Translation: AAH68009.1.
    AF078843 mRNA. Translation: AAF23354.1. Different initiation.
    CCDSiCCDS8655.1. [Q9H0S4-1]
    CCDS8656.1. [Q9H0S4-2]
    RefSeqiNP_057439.2. NM_016355.3. [Q9H0S4-1]
    NP_957518.1. NM_201224.1. [Q9H0S4-2]
    UniGeneiHs.719938.

    Genome annotation databases

    EnsembliENST00000352940; ENSP00000319578; ENSG00000213782. [Q9H0S4-2]
    ENST00000358007; ENSP00000350698; ENSG00000213782. [Q9H0S4-1]
    GeneIDi51202.
    KEGGihsa:51202.
    UCSCiuc001rav.3. human. [Q9H0S4-1]
    uc001ray.3. human.

    Polymorphism databases

    DMDMi52782792.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136666 mRNA. Translation: CAB66601.1 .
    AK054574 mRNA. Translation: BAB70762.1 .
    AK127712 mRNA. Translation: BAG54556.1 .
    AC007215 Genomic DNA. No translation available.
    CH471094 Genomic DNA. Translation: EAW96277.1 .
    CH471094 Genomic DNA. Translation: EAW96283.1 .
    BC009379 mRNA. Translation: AAH09379.2 .
    BC068009 mRNA. Translation: AAH68009.1 .
    AF078843 mRNA. Translation: AAF23354.1 . Different initiation.
    CCDSi CCDS8655.1. [Q9H0S4-1 ]
    CCDS8656.1. [Q9H0S4-2 ]
    RefSeqi NP_057439.2. NM_016355.3. [Q9H0S4-1 ]
    NP_957518.1. NM_201224.1. [Q9H0S4-2 ]
    UniGenei Hs.719938.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BER X-ray 1.40 A 5-230 [» ]
    ProteinModelPortali Q9H0S4.
    SMRi Q9H0S4. Positions 11-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119375. 18 interactions.
    IntActi Q9H0S4. 13 interactions.
    MINTi MINT-3056694.
    STRINGi 9606.ENSP00000350698.

    PTM databases

    PhosphoSitei Q9H0S4.

    Polymorphism databases

    DMDMi 52782792.

    2D gel databases

    SWISS-2DPAGE Q9H0S4.

    Proteomic databases

    MaxQBi Q9H0S4.
    PaxDbi Q9H0S4.
    PRIDEi Q9H0S4.

    Protocols and materials databases

    DNASUi 51202.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000352940 ; ENSP00000319578 ; ENSG00000213782 . [Q9H0S4-2 ]
    ENST00000358007 ; ENSP00000350698 ; ENSG00000213782 . [Q9H0S4-1 ]
    GeneIDi 51202.
    KEGGi hsa:51202.
    UCSCi uc001rav.3. human. [Q9H0S4-1 ]
    uc001ray.3. human.

    Organism-specific databases

    CTDi 51202.
    GeneCardsi GC12P012966.
    HGNCi HGNC:18682. DDX47.
    HPAi HPA014855.
    MIMi 615428. gene.
    neXtProti NX_Q9H0S4.
    PharmGKBi PA134918403.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0513.
    HOGENOMi HOG000268802.
    HOVERGENi HBG100512.
    InParanoidi Q9H0S4.
    KOi K14777.
    OMAi NKFRAGS.
    OrthoDBi EOG7GTT3T.
    PhylomeDBi Q9H0S4.
    TreeFami TF105714.

    Miscellaneous databases

    ChiTaRSi DDX47. human.
    EvolutionaryTracei Q9H0S4.
    GeneWikii DDX47.
    GenomeRNAii 51202.
    NextBioi 54238.
    PROi Q9H0S4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9H0S4.
    CleanExi HS_DDX47.
    Genevestigatori Q9H0S4.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORM 1).
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [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] (ISOFORM 1).
      Tissue: Brain and Eye.
    6. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-24; 75-102; 142-161; 170-190; 238-248; 285-301; 315-325; 378-384 AND 424-441, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    7. "Functional prediction of the coding sequences of 50 new genes deduced by analysis of cDNA clones from human fetal liver."
      Yu Y., Zhang C., Luo L., Ouyang S., Zhang S., Li W., Wu J., Zhou S., Liu M., He F.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-455 (ISOFORM 2).
      Tissue: Liver.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "GABAA receptor-associated protein (GABARAP) induces apoptosis by interacting with DEAD (Asp-Glu-Ala-Asp/His) box polypeptide 47 (DDX 47)."
      Lee J.H., Rho S.B., Chun T.
      Biotechnol. Lett. 27:623-628(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GABARAP, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "NOP132 is required for proper nucleolus localization of DEAD-box RNA helicase DDX47."
      Sekiguchi T., Hayano T., Yanagida M., Takahashi N., Nishimoto T.
      Nucleic Acids Res. 34:4593-4608(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NOL8, SUBCELLULAR LOCATION.
    12. "Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
      Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
      EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AGO1 AND AGO2.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-230 IN COMPLEX WITH AMP.

    Entry informationi

    Entry nameiDDX47_HUMAN
    AccessioniPrimary (citable) accession number: Q9H0S4
    Secondary accession number(s): B3KXP4
    , G5E955, Q96GM0, Q96NV8, Q9UI98
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 125 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3