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Q92841

- DDX17_HUMAN

UniProt

Q92841 - DDX17_HUMAN

Protein

Probable ATP-dependent RNA helicase DDX17

Gene

DDX17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (21 Mar 2012)
      Previous versions | rss
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    Functioni

    RNA-dependent ATPase activity. Involved in transcriptional regulation. Transcriptional coactivator for estrogen receptor ESR1. Increases ESR1 AF-1 domain-mediated transactivation. Synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and probably involved in skeletal muscle differentiation. Required for zinc-finger antiviral protein ZC3HAV1-mediated mRNA degradation.6 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi215 – 2228ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. positive regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
    3. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    4. regulation of skeletal muscle cell differentiation Source: UniProtKB
    5. RNA processing Source: ProtInc
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable ATP-dependent RNA helicase DDX17 (EC:3.6.4.13)
    Alternative name(s):
    DEAD box protein 17
    DEAD box protein p72
    RNA-dependent helicase p72
    Gene namesi
    Name:DDX17
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:2740. DDX17.

    Subcellular locationi

    Nucleus 1 Publication. Nucleusnucleolus 1 Publication

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. nucleolus Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi129 – 1291K → R: Impaired sumoylation and decreased stability. 1 Publication

    Organism-specific databases

    PharmGKBiPA27206.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 729729Probable ATP-dependent RNA helicase DDX17PRO_0000054993Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei64 – 641Phosphoserine1 Publication
    Cross-linki129 – 129Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei523 – 5231Phosphothreonine1 Publication

    Post-translational modificationi

    Sumoylation significantly increases stability, it also promotes interaction with HDAC1.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ92841.
    PaxDbiQ92841.
    PRIDEiQ92841.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00023785.

    PTM databases

    PhosphoSiteiQ92841.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ92841.
    BgeeiQ92841.
    CleanExiHS_DDX17.
    GenevestigatoriQ92841.

    Organism-specific databases

    HPAiCAB024908.
    HPA051161.

    Interactioni

    Subunit structurei

    Interacts with ESR1. Interacts with NCOA1, NCOA2, NCOA3, TP53 and HDAC1. Self-associates. Interacts with DDX5. Interacts with DCP1A in an RNA-independent manner. Interacts with DCP2 in an RNA-dependent manner. Interacts with ZC3HAV1 (via N-terminal domain) in an RNA-independent manner. Interacts with EXOSC3 and EXOSC5 only in the presence of ZC3HAV1 in an RNA-independent manner.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DDX5P178443EBI-746012,EBI-351962
    ESR1P033727EBI-746012,EBI-78473
    HDAC1Q135473EBI-5280703,EBI-301834
    NCOA2Q155962EBI-746012,EBI-81236
    NCOA3Q9Y6Q92EBI-746012,EBI-81196
    NFAT5O949163EBI-746012,EBI-308320
    Srek1Q9JKL73EBI-746012,EBI-6452221From a different organism.
    TP53P046373EBI-746012,EBI-366083
    YAP1P469377EBI-746012,EBI-1044059

    Protein-protein interaction databases

    BioGridi115776. 100 interactions.
    DIPiDIP-29843N.
    IntActiQ92841. 59 interactions.
    MINTiMINT-4545892.
    STRINGi9606.ENSP00000380033.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92841.
    SMRiQ92841. Positions 126-546.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini202 – 377176Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini405 – 552148Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni547 – 729183Transactivation domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi171 – 19929Q motifAdd
    BLAST
    Motifi325 – 3284DEAD box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi101 – 1044Poly-Gly
    Compositional biasi556 – 5638Poly-Gly
    Compositional biasi718 – 7269Poly-Pro

    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.
    InParanoidiQ92841.
    KOiK13178.

    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. Align

    Isoform 1 (identifier: Q92841-4) [UniParc]FASTAAdd to Basket

    Also known as: p82

    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

    MPTGFVAPIL CVLLPSPTRE AATVASATGD SASERESAAP AAAPTAEAPP    50
    PSVVTRPEPQ ALPSPAIRAP LPDLYPFGTM RGGGFGDRDR DRDRGGFGAR 100
    GGGGLPPKKF GNPGERLRKK KWDLSELPKF EKNFYVEHPE VARLTPYEVD 150
    ELRRKKEITV RGGDVCPKPV FAFHHANFPQ YVMDVLMDQH FTEPTPIQCQ 200
    GFPLALSGRD MVGIAQTGSG KTLAYLLPAI VHINHQPYLE RGDGPICLVL 250
    APTRELAQQV QQVADDYGKC SRLKSTCIYG GAPKGPQIRD LERGVEICIA 300
    TPGRLIDFLE SGKTNLRRCT YLVLDEADRM LDMGFEPQIR KIVDQIRPDR 350
    QTLMWSATWP KEVRQLAEDF LRDYTQINVG NLELSANHNI LQIVDVCMES 400
    EKDHKLIQLM EEIMAEKENK TIIFVETKRR CDDLTRRMRR DGWPAMCIHG 450
    DKSQPERDWV LNEFRSGKAP ILIATDVASR GLDVEDVKFV INYDYPNSSE 500
    DYVHRIGRTA RSTNKGTAYT FFTPGNLKQA RELIKVLEEA NQAINPKLMQ 550
    LVDHRGGGGG GGGRSRYRTT SSANNPNLMY QDECDRRLRG VKDGGRRDSA 600
    SYRDRSETDR AGYANGSGYG SPNSAFGAQA GQYTYGQGTY GAAAYGTSSY 650
    TAQEYGAGTY GASSTTSTGR SSQSSSQQFS GIGRSGQQPQ PLMSQQFAQP 700
    PGATNMIGYM GQTAYQYPPP PPPPPPSRK 729

    Note: Starts at an alternative CUG codon.

    Length:729
    Mass (Da):80,272
    Last modified:March 21, 2012 - v2
    Checksum:iC819F53515B1BC39
    GO
    Isoform 2 (identifier: Q92841-1) [UniParc]FASTAAdd to Basket

    Also known as: p72

    The sequence of this isoform differs from the canonical sequence as follows:
         1-79: Missing.

    Note: Produced by alternative initiation at Met-80 of isoform 1.

    Show »
    Length:650
    Mass (Da):72,371
    Checksum:iE58AA249D23F66F3
    GO
    Isoform 3 (identifier: Q92841-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-79: Missing.
         482-482: L → LGL

    Note: Produced by alternative splicing of isoform 2. No experimental confirmation available.

    Show »
    Length:652
    Mass (Da):72,542
    Checksum:i71E89198BBDBF2E6
    GO
    Isoform 4 (identifier: Q92841-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-79: Missing.
         562-562: G → GKG

    Note: Produced by alternative splicing of isoform 2. No experimental confirmation available.

    Show »
    Length:652
    Mass (Da):72,557
    Checksum:i05DFD042E4268F2C
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7979Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_042527Add
    BLAST
    Alternative sequencei482 – 4821L → LGL in isoform 3. 1 PublicationVSP_042528
    Alternative sequencei562 – 5621G → GKG in isoform 4. 1 PublicationVSP_042529

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59321 mRNA. Translation: AAC50787.1.
    CR456432 mRNA. Translation: CAG30318.1.
    AL713763 mRNA. Translation: CAH10627.2.
    Z97056 Genomic DNA. Translation: CAQ08924.1.
    Z97056 Genomic DNA. Translation: CAB09792.1.
    CH471095 Genomic DNA. Translation: EAW60243.1.
    BC000595 mRNA. Translation: AAH00595.2.
    CCDSiCCDS33646.1. [Q92841-4]
    PIRiS72367.
    RefSeqiNP_006377.2. NM_006386.4. [Q92841-4]
    UniGeneiHs.528305.
    Hs.706116.

    Genome annotation databases

    EnsembliENST00000403230; ENSP00000385536; ENSG00000100201.
    GeneIDi10521.
    KEGGihsa:10521.
    UCSCiuc003avx.4. human. [Q92841-4]

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59321 mRNA. Translation: AAC50787.1 .
    CR456432 mRNA. Translation: CAG30318.1 .
    AL713763 mRNA. Translation: CAH10627.2 .
    Z97056 Genomic DNA. Translation: CAQ08924.1 .
    Z97056 Genomic DNA. Translation: CAB09792.1 .
    CH471095 Genomic DNA. Translation: EAW60243.1 .
    BC000595 mRNA. Translation: AAH00595.2 .
    CCDSi CCDS33646.1. [Q92841-4 ]
    PIRi S72367.
    RefSeqi NP_006377.2. NM_006386.4. [Q92841-4 ]
    UniGenei Hs.528305.
    Hs.706116.

    3D structure databases

    ProteinModelPortali Q92841.
    SMRi Q92841. Positions 126-546.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115776. 100 interactions.
    DIPi DIP-29843N.
    IntActi Q92841. 59 interactions.
    MINTi MINT-4545892.
    STRINGi 9606.ENSP00000380033.

    PTM databases

    PhosphoSitei Q92841.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00023785.

    Proteomic databases

    MaxQBi Q92841.
    PaxDbi Q92841.
    PRIDEi Q92841.

    Protocols and materials databases

    DNASUi 10521.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000403230 ; ENSP00000385536 ; ENSG00000100201 .
    GeneIDi 10521.
    KEGGi hsa:10521.
    UCSCi uc003avx.4. human. [Q92841-4 ]

    Organism-specific databases

    CTDi 10521.
    GeneCardsi GC22M038879.
    HGNCi HGNC:2740. DDX17.
    HPAi CAB024908.
    HPA051161.
    MIMi 608469. gene.
    neXtProti NX_Q92841.
    PharmGKBi PA27206.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0513.
    HOGENOMi HOG000268804.
    HOVERGENi HBG015893.
    InParanoidi Q92841.
    KOi K13178.

    Miscellaneous databases

    ChiTaRSi DDX17. human.
    GeneWikii DDX17.
    GenomeRNAii 10521.
    NextBioi 39902.
    PROi Q92841.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92841.
    Bgeei Q92841.
    CleanExi HS_DDX17.
    Genevestigatori Q92841.

    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. "p72: a human nuclear DEAD box protein highly related to p68."
      Lamm G.M., Nicol S.M., Fuller-Pace F.V., Lamond A.I.
      Nucleic Acids Res. 24:3739-3747(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Amygdala.
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Skin.
    7. "The mRNA of DEAD box protein p72 is alternatively translated into an 82-kDa RNA helicase."
      Uhlmann-Schiffler H., Rossler O.G., Stahl H.
      J. Biol. Chem. 277:1066-1075(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE INITIATION (ISOFORM 1).
    8. "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.
    9. "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 DDX5.
    10. "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.
    11. "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: INTERACTION WITH TP53.
    12. "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.
    13. "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.
    14. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Concerted activation of the Mdm2 promoter by p72 RNA helicase and the coactivators p300 and P/CAF."
      Shin S., Janknecht R.
      J. Cell. Biochem. 101:1252-1265(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH EP300; CREBBP AND KAT2B.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "p72 DEAD box RNA helicase is required for optimal function of the zinc-finger antiviral protein."
      Chen G., Guo X., Lv F., Xu Y., Gao G.
      Proc. Natl. Acad. Sci. U.S.A. 105:4352-4357(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ZC3HAV1; EXOSC3 AND EXOSC5.
    19. "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.
    20. "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-129, MUTAGENESIS OF LYS-129.
    21. "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-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation."
      Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G.
      Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DCP1A AND DCP2.
    24. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
      Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
      Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDDX17_HUMAN
    AccessioniPrimary (citable) accession number: Q92841
    Secondary accession number(s): B1AHM0, Q69YT1, Q6ICD6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: March 21, 2012
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 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 22
      Human chromosome 22: 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