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P17844

- DDX5_HUMAN

UniProt

P17844 - DDX5_HUMAN

Protein

Probable ATP-dependent RNA helicase DDX5

Gene

DDX5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for estrogen receptor ESR1 and androgen receptor AR. Increases ESR1 AF-1 domain-mediated transactivation and ESR1 AF-1 and AF-2 domains transcriptional synergistic activity. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specicic manner; the function probbaly involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms.10 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei121 – 1211ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi114 – 1163ATP
    Nucleotide bindingi138 – 1458ATP

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. ATP-dependent RNA helicase activity Source: Ensembl
    4. estrogen receptor binding Source: UniProtKB
    5. poly(A) RNA binding Source: UniProtKB
    6. pre-mRNA binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. RNA helicase activity Source: UniProtKB
    9. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. cell growth Source: UniProtKB
    2. circadian rhythm Source: Ensembl
    3. intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
    4. in utero embryonic development Source: Ensembl
    5. mRNA splicing, via spliceosome Source: UniProtKB
    6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. positive regulation of DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
    8. positive regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
    9. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    10. regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
    11. regulation of androgen receptor signaling pathway Source: UniProtKB
    12. regulation of osteoblast differentiation Source: UniProtKB
    13. regulation of skeletal muscle cell differentiation Source: UniProtKB
    14. regulation of viral genome replication Source: Ensembl
    15. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Biological rhythms, mRNA processing, mRNA splicing, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable ATP-dependent RNA helicase DDX5 (EC:3.6.4.13)
    Alternative name(s):
    DEAD box protein 5
    RNA helicase p68
    Gene namesi
    Name:DDX5
    Synonyms:G17P1, HELR, HLR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:2746. DDX5.

    Subcellular locationi

    Nucleusnucleolus 2 Publications

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB
    4. nucleolus Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. ribonucleoprotein complex Source: MGI

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi53 – 531K → R: Abolishes sumoylation, abolishes interaction with HDAC1, increases TP53 coactivation and promotes polyubiquitination. 2 Publications
    Mutagenesisi55 – 551E → A: Abolishes sumoylation. 1 Publication
    Mutagenesisi144 – 1441K → R: Abolishes RNA helicase activity, no effect on transcriptional coactivator function. 2 Publications
    Mutagenesisi403 – 4031R → L: Binds to the tau stem-loop-containing RNA. Inhibits tau exon 10 inclusion and RNA cleavage. Does not inhibit interaction with RBM4. 1 Publication

    Organism-specific databases

    PharmGKBiPA27228.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 614614Probable ATP-dependent RNA helicase DDX5PRO_0000054991Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321N6-acetyllysine1 Publication
    Modified residuei33 – 331N6-acetyllysine1 Publication
    Modified residuei40 – 401N6-acetyllysine1 Publication
    Cross-linki53 – 53Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei236 – 2361N6-acetyllysineBy similarity
    Modified residuei297 – 2971Phosphotyrosine1 Publication
    Modified residuei480 – 4801Phosphoserine2 Publications

    Post-translational modificationi

    Arg-502 is dimethylated, probably to asymmetric dimethylarginine.
    Sumoylated; sumoylation, promoted by PIAS1, promotes interaction with HDAC1 and transcriptional repression activity. Sumoylation also significantly increases stability, and reduces polyubiquitination.2 Publications
    Polyubiquitinated, leading to proteasomal degradation.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP17844.
    PaxDbiP17844.
    PeptideAtlasiP17844.
    PRIDEiP17844.

    2D gel databases

    SWISS-2DPAGEP17844.

    PTM databases

    PhosphoSiteiP17844.

    Expressioni

    Gene expression databases

    ArrayExpressiP17844.
    BgeeiP17844.
    CleanExiHS_DDX5.
    GenevestigatoriP17844.

    Organism-specific databases

    HPAiCAB005868.
    HPA020043.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex. Interacts with RBM4; the interaction occurs in an RNA-independent manner. Interacts with AGO1 and AGO2. Interacts with ESR1; the interaction is enhanced by phosphorylation of ESR1 AF-1 domain. Interacts with AR, NCOA1, NCOA2, NCOA3, EP300, CREBBP, POLR2A, TP53, RUNX2 and HDAC1. Self-associates. Interacts with DDX17. Interacts with BRDT. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active).16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P2795812EBI-351962,EBI-6904388From a different organism.
    P299913EBI-351962,EBI-8826747From a different organism.
    CHD3Q128734EBI-351962,EBI-523590
    CrebbpP454813EBI-351962,EBI-296306From a different organism.
    DDX17Q928413EBI-351962,EBI-746012
    EBNA-LPQ8AZK72EBI-351962,EBI-1185167From a different organism.
    EP300Q094724EBI-351962,EBI-447295
    ESR1P033728EBI-351962,EBI-78473
    FBLP220876EBI-351962,EBI-358318
    HDAC1Q135474EBI-351962,EBI-301834
    MBD3O959834EBI-351962,EBI-1783068
    Myod1P100853EBI-351962,EBI-4405734From a different organism.
    NFAT5O949164EBI-351962,EBI-308320
    POLR2AP249283EBI-351962,EBI-295301
    Runx2Q08775-32EBI-351962,EBI-6119991From a different organism.
    TP53P046376EBI-351962,EBI-366083
    TP53P04637-12EBI-351962,EBI-3895849
    TP53P04637-72EBI-351962,EBI-3895873

    Protein-protein interaction databases

    BioGridi108021. 159 interactions.
    DIPiDIP-29844N.
    IntActiP17844. 83 interactions.
    MINTiMINT-5000516.
    STRINGi9606.ENSP00000225792.

    Structurei

    Secondary structure

    1
    614
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi64 – 663
    Helixi72 – 809
    Beta strandi82 – 876
    Turni96 – 994
    Helixi103 – 1108
    Turni111 – 1133
    Helixi119 – 13012
    Beta strandi134 – 1385
    Helixi144 – 15714
    Beta strandi169 – 1735
    Helixi177 – 19317
    Beta strandi198 – 2014
    Helixi207 – 21610
    Beta strandi219 – 2235
    Helixi225 – 2339
    Turni234 – 2363
    Beta strandi239 – 2413
    Beta strandi244 – 2474
    Helixi250 – 2556
    Helixi259 – 2668
    Beta strandi274 – 2807
    Helixi284 – 29310
    Beta strandi298 – 3025

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FE2X-ray2.60A/B68-307[»]
    4A4DX-ray2.70A52-304[»]
    ProteinModelPortaliP17844.
    SMRiP17844. Positions 50-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17844.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini125 – 300176Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini328 – 475148Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni477 – 614138Transactivation domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi94 – 12229Q motifAdd
    BLAST
    Motifi248 – 2514DEAD box

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0513.
    HOGENOMiHOG000268804.
    HOVERGENiHBG015893.
    InParanoidiP17844.
    KOiK12823.
    PhylomeDBiP17844.
    TreeFamiTF300332.

    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.
    IPR012587. P68HR.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF08061. P68HR. 2 hits.
    [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.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P17844-1) [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

    MSGYSSDRDR GRDRGFGAPR FGGSRAGPLS GKKFGNPGEK LVKKKWNLDE    50
    LPKFEKNFYQ EHPDLARRTA QEVETYRRSK EITVRGHNCP KPVLNFYEAN 100
    FPANVMDVIA RQNFTEPTAI QAQGWPVALS GLDMVGVAQT GSGKTLSYLL 150
    PAIVHINHQP FLERGDGPIC LVLAPTRELA QQVQQVAAEY CRACRLKSTC 200
    IYGGAPKGPQ IRDLERGVEI CIATPGRLID FLECGKTNLR RTTYLVLDEA 250
    DRMLDMGFEP QIRKIVDQIR PDRQTLMWSA TWPKEVRQLA EDFLKDYIHI 300
    NIGALELSAN HNILQIVDVC HDVEKDEKLI RLMEEIMSEK ENKTIVFVET 350
    KRRCDELTRK MRRDGWPAMG IHGDKSQQER DWVLNEFKHG KAPILIATDV 400
    ASRGLDVEDV KFVINYDYPN SSEDYIHRIG RTARSTKTGT AYTFFTPNNI 450
    KQVSDLISVL REANQAINPK LLQLVEDRGS GRSRGRGGMK DDRRDRYSAG 500
    KRGGFNTFRD RENYDRGYSS LLKRDFGAKT QNGVYSAANY TNGSFGSNFV 550
    SAGIQTSFRT GNPTGTYQNG YDSTQQYGSN VPNMHNGMNQ QAYAYPATAA 600
    APMIGYPMPT GYSQ 614
    Length:614
    Mass (Da):69,148
    Last modified:August 1, 1990 - v1
    Checksum:i84DF684FD6871594
    GO
    Isoform 2 (identifier: P17844-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         85-163: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:535
    Mass (Da):60,563
    Checksum:iA665AD0571ABC456
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti480 – 4801S → A.
    Corresponds to variant rs1140409 [ dbSNP | Ensembl ].
    VAR_029241

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei85 – 16379Missing in isoform 2. 1 PublicationVSP_056154Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52104 mRNA. Translation: CAA36324.1.
    AF015812 Genomic DNA. Translation: AAB84094.1.
    BT006943 mRNA. Translation: AAP35589.1.
    AK297192 mRNA. Translation: BAG59680.1.
    AB451257 mRNA. Translation: BAG70071.1.
    AC009994 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94202.1.
    CH471109 Genomic DNA. Translation: EAW94203.1.
    BC016027 mRNA. Translation: AAH16027.1.
    X15729 mRNA. Translation: CAA33751.1.
    AJ010931 Genomic DNA. Translation: CAA09408.1.
    CCDSiCCDS11659.1.
    PIRiJC1087.
    RefSeqiNP_004387.1. NM_004396.3.
    XP_005257168.1. XM_005257111.1.
    XP_006721801.1. XM_006721738.1.
    UniGeneiHs.279806.

    Genome annotation databases

    EnsembliENST00000225792; ENSP00000225792; ENSG00000108654.
    ENST00000450599; ENSP00000403085; ENSG00000108654.
    GeneIDi1655.
    KEGGihsa:1655.
    UCSCiuc002jej.2. human.

    Polymorphism databases

    DMDMi129383.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52104 mRNA. Translation: CAA36324.1 .
    AF015812 Genomic DNA. Translation: AAB84094.1 .
    BT006943 mRNA. Translation: AAP35589.1 .
    AK297192 mRNA. Translation: BAG59680.1 .
    AB451257 mRNA. Translation: BAG70071.1 .
    AC009994 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94202.1 .
    CH471109 Genomic DNA. Translation: EAW94203.1 .
    BC016027 mRNA. Translation: AAH16027.1 .
    X15729 mRNA. Translation: CAA33751.1 .
    AJ010931 Genomic DNA. Translation: CAA09408.1 .
    CCDSi CCDS11659.1.
    PIRi JC1087.
    RefSeqi NP_004387.1. NM_004396.3.
    XP_005257168.1. XM_005257111.1.
    XP_006721801.1. XM_006721738.1.
    UniGenei Hs.279806.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FE2 X-ray 2.60 A/B 68-307 [» ]
    4A4D X-ray 2.70 A 52-304 [» ]
    ProteinModelPortali P17844.
    SMRi P17844. Positions 50-473.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108021. 159 interactions.
    DIPi DIP-29844N.
    IntActi P17844. 83 interactions.
    MINTi MINT-5000516.
    STRINGi 9606.ENSP00000225792.

    PTM databases

    PhosphoSitei P17844.

    Polymorphism databases

    DMDMi 129383.

    2D gel databases

    SWISS-2DPAGE P17844.

    Proteomic databases

    MaxQBi P17844.
    PaxDbi P17844.
    PeptideAtlasi P17844.
    PRIDEi P17844.

    Protocols and materials databases

    DNASUi 1655.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000225792 ; ENSP00000225792 ; ENSG00000108654 .
    ENST00000450599 ; ENSP00000403085 ; ENSG00000108654 .
    GeneIDi 1655.
    KEGGi hsa:1655.
    UCSCi uc002jej.2. human.

    Organism-specific databases

    CTDi 1655.
    GeneCardsi GC17M062494.
    HGNCi HGNC:2746. DDX5.
    HPAi CAB005868.
    HPA020043.
    MIMi 180630. gene.
    neXtProti NX_P17844.
    PharmGKBi PA27228.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0513.
    HOGENOMi HOG000268804.
    HOVERGENi HBG015893.
    InParanoidi P17844.
    KOi K12823.
    PhylomeDBi P17844.
    TreeFami TF300332.

    Miscellaneous databases

    ChiTaRSi DDX5. human.
    EvolutionaryTracei P17844.
    GeneWikii DDX5.
    GenomeRNAii 1655.
    NextBioi 6816.
    PROi P17844.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17844.
    Bgeei P17844.
    CleanExi HS_DDX5.
    Genevestigatori P17844.

    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.
    IPR012587. P68HR.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF08061. P68HR. 2 hits.
    [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. "Complete cDNA sequence of the human p68 protein."
      Hloch P., Stahl H.
      Nucleic Acids Res. 18:3045-3045(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "p68 RNA helicase: identification of a nucleolar form and cloning of related genes containing a conserved intron in yeasts."
      Iggo R.D., Jamieson D.J., McNeill S.A., Southgate J., McPheat J., Lane D.P.
      Mol. Cell. Biol. 11:1326-1333(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
    3. "Structure and expression of the human p68 RNA helicase gene."
      Roessler O.G., Hloch P., Schutz N., Weitzenegger T., Stahl H.
      Nucleic Acids Res. 28:932-939(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "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 2).
      Tissue: Brain.
    6. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Muscle.
    10. "Nuclear protein with sequence homology to translation initiation factor eIF-4A."
      Ford M.J., Anton I.A., Lane D.P.
      Nature 332:736-738(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-614 (ISOFORM 1).
    11. "Molecular organization of the murine p68 RNA helicase gene promotor region."
      Petry P., Bammer S., Heinlein U.A.O.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-163.
    12. "Purification and identification of p68 RNA helicase acting as a transcriptional coactivator specific for the activation function 1 of human estrogen receptor alpha."
      Endoh H., Maruyama K., Masuhiro Y., Kobayashi Y., Goto M., Tai H., Yanagisawa J., Metzger D., Hashimoto S., Kato S.
      Mol. Cell. Biol. 19:5363-5372(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH ESR1, MUTAGENESIS OF LYS-144.
    13. "The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase."
      Nicol S.M., Causevic M., Prescott A.R., Fuller-Pace F.V.
      Exp. Cell Res. 257:272-280(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FBL, SUBCELLULAR LOCATION.
    14. "A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor alpha coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA."
      Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S., Arao Y., Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y., Kato S.
      EMBO J. 20:1341-1352(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH ESR1; NCOA1; NCOA2 AND NCOA3.
    15. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    16. "The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells."
      Ogilvie V.C., Wilson B.J., Nicol S.M., Morrice N.A., Saunders L.R., Barber G.N., Fuller-Pace F.V.
      Nucleic Acids Res. 31:1470-1480(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SELF-ASSOCIATION, INTERACTION WITH DDX17.
    17. "Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300."
      Rossow K.L., Janknecht R.
      Oncogene 22:151-156(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH EP300; CREBBP AND POLR2A.
    18. "The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner."
      Wilson B.J., Bates G.J., Nicol S.M., Gregory D.J., Perkins N.D., Fuller-Pace F.V.
      BMC Mol. Biol. 5:11-11(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTIONAL REPRESSION, INTERACTION WITH HDAC1.
    19. "The DEAD box protein p68: a novel transcriptional coactivator of the p53 tumour suppressor."
      Bates G.J., Nicol S.M., Wilson B.J., Jacobs A.M., Bourdon J.C., Wardrop J., Gregory D.J., Lane D.P., Perkins N.D., Fuller-Pace F.V.
      EMBO J. 24:543-553(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH TP53.
    20. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "The RNA helicases p68/p72 and the noncoding RNA SRA are coregulators of MyoD and skeletal muscle differentiation."
      Caretti G., Schiltz R.L., Dilworth F.J., Di Padova M., Zhao P., Ogryzko V., Fuller-Pace F.V., Hoffman E.P., Tapscott S.J., Sartorelli V.
      Dev. Cell 11:547-560(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MYOD1, MUTAGENESIS OF LYS-144.
    22. "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.
    23. "SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1."
      Jacobs A.M., Nicol S.M., Hislop R.G., Jaffray E.G., Hay R.T., Fuller-Pace F.V.
      Oncogene 26:5866-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-53, INTERACTION WITH HDAC1 AND PIAS1, MUTAGENESIS OF LYS-53 AND GLU-55.
    24. "The RNA helicase p68 is a novel androgen receptor coactivator involved in splicing and is overexpressed in prostate cancer."
      Clark E.L., Coulson A., Dalgliesh C., Rajan P., Nicol S.M., Fleming S., Heer R., Gaughan L., Leung H.Y., Elliott D.J., Fuller-Pace F.V., Robson C.N.
      Cancer Res. 68:7938-7946(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH AR.
    25. Cited for: FUNCTION, INTERACTION WITH RUNX2.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. "The DEAD-box protein p72 regulates ERalpha-/oestrogen-dependent transcription and cell growth, and is associated with improved survival in ERalpha-positive breast cancer."
      Wortham N.C., Ahamed E., Nicol S.M., Thomas R.S., Periyasamy M., Jiang J., Ochocka A.M., Shousha S., Huson L., Bray S.E., Coombes R.C., Ali S., Fuller-Pace F.V.
      Oncogene 28:4053-4064(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ESR1.
    28. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-33 AND LYS-40, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Sumoylation of p68 and p72 RNA helicases affects protein stability and transactivation potential."
      Mooney S.M., Grande J.P., Salisbury J.L., Janknecht R.
      Biochemistry 49:1-10(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-53, MUTAGENESIS OF LYS-53, POLYUBIQUITINATION.
    30. "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-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "RNA helicase p68 (DDX5) regulates tau exon 10 splicing by modulating a stem-loop structure at the 5' splice site."
      Kar A., Fushimi K., Zhou X., Ray P., Shi C., Chen X., Liu Z., Chen S., Wu J.Y.
      Mol. Cell. Biol. 31:1812-1821(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RBM4, MUTAGENESIS OF ARG-403, RNA-BINDING.
    33. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 68-307 IN COMPLEX WITH ADP.

    Entry informationi

    Entry nameiDDX5_HUMAN
    AccessioniPrimary (citable) accession number: P17844
    Secondary accession number(s): B4DLW8
    , B5BU21, D3DU32, E7ETL9, O75681, Q53Y61
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 168 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, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3