DDX17_HUMAN
ID DDX17_HUMAN Reviewed; 729 AA.
AC Q92841; B1AHM0; H3BLZ8; Q69YT1; Q6ICD6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX17;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 17;
DE AltName: Full=DEAD box protein p72;
DE AltName: Full=DEAD box protein p82 {ECO:0000303|PubMed:19995069};
DE AltName: Full=RNA-dependent helicase p72;
GN Name=DDX17;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=8871553; DOI=10.1093/nar/24.19.3739;
RA Lamm G.M., Nicol S.M., Fuller-Pace F.V., Lamond A.I.;
RT "p72: a human nuclear DEAD box protein highly related to p68.";
RL Nucleic Acids Res. 24:3739-3747(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 36-81; 122-154; 210-241; 255-269; 305-313; 365-372;
RP 406-417; 421-428; 458-480; 489-505; 516-528; 536-547; 569-587 AND 671-684,
RP INTERACTION WITH CDK9, AND FUNCTION IN ALTERNATIVE SPLICING.
RX PubMed=26209609; DOI=10.1074/mcp.m115.049221;
RA Yang J., Zhao Y., Kalita M., Li X., Jamaluddin M., Tian B., Edeh C.B.,
RA Wiktorowicz J.E., Kudlicki A., Brasier A.R.;
RT "Systematic determination of human cyclin dependent kinase (CDK)-9
RT interactome identifies novel functions in RNA splicing mediated by the DEAD
RT box (DDX)-5/17 RNA helicases.";
RL Mol. Cell. Proteomics 14:2701-2721(2015).
RN [8]
RP PROTEIN SEQUENCE OF 305-314, MASS SPECTROMETRY, FUNCTION, AND INTERACTION
RP WITH MYOD1.
RX PubMed=17011493; DOI=10.1016/j.devcel.2006.08.003;
RA Caretti G., Schiltz R.L., Dilworth F.J., Di Padova M., Zhao P., Ogryzko V.,
RA Fuller-Pace F.V., Hoffman E.P., Tapscott S.J., Sartorelli V.;
RT "The RNA helicases p68/p72 and the noncoding RNA SRA are coregulators of
RT MyoD and skeletal muscle differentiation.";
RL Dev. Cell 11:547-560(2006).
RN [9]
RP CAUTION.
RX PubMed=11250900; DOI=10.1093/emboj/20.6.1341;
RA Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S., Arao Y.,
RA Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y., Kato S.;
RT "A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor
RT alpha coactivator through the N-terminal activation domain (AF-1) with an
RT RNA coactivator, SRA.";
RL EMBO J. 20:1341-1352(2001).
RN [10]
RP ERRATUM OF PUBMED:11250900, AND RETRACTION NOTICE OF PUBMED:11250900.
RX PubMed=25452582; DOI=10.15252/embj.201470090;
RA Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S., Arao Y.,
RA Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y., Kato S.;
RL EMBO J. 33:2880-2880(2014).
RN [11]
RP ALTERNATIVE INITIATION (ISOFORM 1).
RX PubMed=11675387; DOI=10.1074/jbc.m107535200;
RA Uhlmann-Schiffler H., Rossler O.G., Stahl H.;
RT "The mRNA of DEAD box protein p72 is alternatively translated into an 82-
RT kDa RNA helicase.";
RL J. Biol. Chem. 277:1066-1075(2002).
RN [12]
RP FUNCTION IN ALTERNATIVE SPLICING, MUTAGENESIS OF LYS-221; THR-222; ASP-328;
RP TRP-355 AND SER-356, AND SUBCELLULAR LOCATION.
RX PubMed=12138182; DOI=10.1128/mcb.22.16.5698-5707.2002;
RA Hoenig A., Auboeuf D., Parker M.M., O'Malley B.W., Berget S.M.;
RT "Regulation of alternative splicing by the ATP-dependent DEAD-box RNA
RT helicase p72.";
RL Mol. Cell. Biol. 22:5698-5707(2002).
RN [13]
RP INTERACTION WITH DDX5, AND SUBCELLULAR LOCATION.
RX PubMed=12595555; DOI=10.1093/nar/gkg236;
RA Ogilvie V.C., Wilson B.J., Nicol S.M., Morrice N.A., Saunders L.R.,
RA Barber G.N., Fuller-Pace F.V.;
RT "The highly related DEAD box RNA helicases p68 and p72 exist as
RT heterodimers in cells.";
RL Nucleic Acids Res. 31:1470-1480(2003).
RN [14]
RP FUNCTION IN TRANSCRIPTIONAL REPRESSION, AND INTERACTION WITH HDAC1.
RX PubMed=15298701; DOI=10.1186/1471-2199-5-11;
RA Wilson B.J., Bates G.J., Nicol S.M., Gregory D.J., Perkins N.D.,
RA Fuller-Pace F.V.;
RT "The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress
RT transcription in a promoter-specific manner.";
RL BMC Mol. Biol. 5:11-11(2004).
RN [15]
RP IDENTIFICATION IN A COMPLEX CONTAINING DROSHA.
RX PubMed=15531877; DOI=10.1038/nature03120;
RA Gregory R.I., Yan K.-P., Amuthan G., Chendrimada T., Doratotaj B.,
RA Cooch N., Shiekhattar R.;
RT "The microprocessor complex mediates the genesis of microRNAs.";
RL Nature 432:235-240(2004).
RN [16]
RP INTERACTION WITH TP53.
RX PubMed=15660129; DOI=10.1038/sj.emboj.7600550;
RA Bates G.J., Nicol S.M., Wilson B.J., Jacobs A.M., Bourdon J.C., Wardrop J.,
RA Gregory D.J., Lane D.P., Perkins N.D., Fuller-Pace F.V.;
RT "The DEAD box protein p68: a novel transcriptional coactivator of the p53
RT tumour suppressor.";
RL EMBO J. 24:543-553(2005).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-523, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [19]
RP FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH CTNNB1,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17699760; DOI=10.1158/0008-5472.can-06-4652;
RA Shin S., Rossow K.L., Grande J.P., Janknecht R.;
RT "Involvement of RNA helicases p68 and p72 in colon cancer.";
RL Cancer Res. 67:7572-7578(2007).
RN [20]
RP FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH EP300; CREBBP AND
RP KAT2B, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-221.
RX PubMed=17226766; DOI=10.1002/jcb.21250;
RA Shin S., Janknecht R.;
RT "Concerted activation of the Mdm2 promoter by p72 RNA helicase and the
RT coactivators p300 and P/CAF.";
RL J. Cell. Biochem. 101:1252-1265(2007).
RN [21]
RP FUNCTION.
RX PubMed=17485482; DOI=10.1093/nar/gkm058;
RA Jalal C., Uhlmann-Schiffler H., Stahl H.;
RT "Redundant role of DEAD box proteins p68 (Ddx5) and p72/p82 (Ddx17) in
RT ribosome biogenesis and cell proliferation.";
RL Nucleic Acids Res. 35:3590-3601(2007).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [23]
RP INTERACTION WITH DHX36.
RX PubMed=18279852; DOI=10.1016/j.yexcr.2008.01.006;
RA Iwamoto F., Stadler M., Chalupnikova K., Oakeley E., Nagamine Y.;
RT "Transcription-dependent nucleolar cap localization and possible nuclear
RT function of DExH RNA helicase RHAU.";
RL Exp. Cell Res. 314:1378-1391(2008).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [25]
RP FUNCTION, INTERACTION WITH ZC3HAV1; EXOSC3 AND EXOSC5, AND MUTAGENESIS OF
RP LYS-221.
RX PubMed=18334637; DOI=10.1073/pnas.0712276105;
RA Chen G., Guo X., Lv F., Xu Y., Gao G.;
RT "p72 DEAD box RNA helicase is required for optimal function of the zinc-
RT finger antiviral protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:4352-4357(2008).
RN [26]
RP FUNCTION, INTERACTION WITH ESR1, AND MUTAGENESIS OF ASP-325.
RX PubMed=19718048; DOI=10.1038/onc.2009.261;
RA Wortham N.C., Ahamed E., Nicol S.M., Thomas R.S., Periyasamy M., Jiang J.,
RA Ochocka A.M., Shousha S., Huson L., Bray S.E., Coombes R.C., Ali S.,
RA Fuller-Pace F.V.;
RT "The DEAD-box protein p72 regulates ERalpha-/oestrogen-dependent
RT transcription and cell growth, and is associated with improved survival in
RT ERalpha-positive breast cancer.";
RL Oncogene 28:4053-4064(2009).
RN [27]
RP FUNCTION, SUMOYLATION AT LYS-129, MUTAGENESIS OF LYS-129, INTERACTION WITH
RP DDX5; HDAC1; HDAC2; HDAC3; EP300 AND ESR1, AND SUBCELLULAR LOCATION.
RX PubMed=19995069; DOI=10.1021/bi901263m;
RA Mooney S.M., Grande J.P., Salisbury J.L., Janknecht R.;
RT "Sumoylation of p68 and p72 RNA helicases affects protein stability and
RT transactivation potential.";
RL Biochemistry 49:1-10(2010).
RN [28]
RP FUNCTION IN ESTROGEN SIGNALING PATHWAY.
RX PubMed=20406972; DOI=10.1158/0008-5472.can-09-3988;
RA Dutertre M., Gratadou L., Dardenne E., Germann S., Samaan S., Lidereau R.,
RA Driouch K., de la Grange P., Auboeuf D.;
RT "Estrogen regulation and physiopathologic significance of alternative
RT promoters in breast cancer.";
RL Cancer Res. 70:3760-3770(2010).
RN [29]
RP FUNCTION, INTERACTION WITH ESR1; HDAC1; HDAC2 AND HDAC3, ACETYLATION AT
RP LYS-108; LYS-109 AND LYS-121, MASS SPECTROMETRY, AND MUTAGENESIS OF
RP 108-LYS-LYS-109 AND LYS-121.
RX PubMed=20663877; DOI=10.1074/jbc.m110.143792;
RA Mooney S.M., Goel A., D'Assoro A.B., Salisbury J.L., Janknecht R.;
RT "Pleiotropic effects of p300-mediated acetylation on p68 and p72 RNA
RT helicase.";
RL J. Biol. Chem. 285:30443-30452(2010).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [32]
RP INTERACTION WITH DCP1A AND DCP2.
RX PubMed=21876179; DOI=10.1073/pnas.1101676108;
RA Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T.,
RA Gao G.;
RT "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively
RT targeting multiply spliced viral mRNAs for degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011).
RN [33]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [34]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=22002106; DOI=10.1074/mcp.m111.013680;
RA Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
RT "Systematic analysis of protein pools, isoforms, and modifications
RT affecting turnover and subcellular localization.";
RL Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
RN [35]
RP FUNCTION IN ALTERNATIVE SPLICING.
RX PubMed=23022728; DOI=10.1038/nsmb.2390;
RA Dardenne E., Pierredon S., Driouch K., Gratadou L., Lacroix-Triki M.,
RA Espinoza M.P., Zonta E., Germann S., Mortada H., Villemin J.P.,
RA Dutertre M., Lidereau R., Vagner S., Auboeuf D.;
RT "Splicing switch of an epigenetic regulator by RNA helicases promotes
RT tumor-cell invasiveness.";
RL Nat. Struct. Mol. Biol. 19:1139-1146(2012).
RN [36]
RP FUNCTION, AND INTERACTION WITH NFAT5.
RX PubMed=22266867; DOI=10.1038/onc.2011.618;
RA Germann S., Gratadou L., Zonta E., Dardenne E., Gaudineau B., Fougere M.,
RA Samaan S., Dutertre M., Jauliac S., Auboeuf D.;
RT "Dual role of the ddx5/ddx17 RNA helicases in the control of the pro-
RT migratory NFAT5 transcription factor.";
RL Oncogene 31:4536-4549(2012).
RN [37]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [38]
RP INTERACTION WITH UPF3B.
RX PubMed=23788676; DOI=10.1093/nar/gkt538;
RA Geissler V., Altmeyer S., Stein B., Uhlmann-Schiffler H., Stahl H.;
RT "The RNA helicase Ddx5/p68 binds to hUpf3 and enhances NMD of Ddx17/p72 and
RT Smg5 mRNA.";
RL Nucleic Acids Res. 41:7875-7888(2013).
RN [39]
RP INTERACTION WITH DGCR8.
RX PubMed=24589731; DOI=10.1016/j.bbrc.2014.02.104;
RA Jung E., Seong Y., Seo J.H., Kwon Y.S., Song H.;
RT "Cell cycle-dependent regulation of Aurora kinase B mRNA by the
RT Microprocessor complex.";
RL Biochem. Biophys. Res. Commun. 446:241-247(2014).
RN [40]
RP FUNCTION IN MICRORNA MATURATION, INTERACTION WITH DROSHA; DGCR8 AND YAP1,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-129.
RX PubMed=24581491; DOI=10.1016/j.cell.2013.12.043;
RA Mori M., Triboulet R., Mohseni M., Schlegelmilch K., Shrestha K.,
RA Camargo F.D., Gregory R.I.;
RT "Hippo signaling regulates microprocessor and links cell-density-dependent
RT miRNA biogenesis to cancer.";
RL Cell 156:893-906(2014).
RN [41]
RP FUNCTION IN ANTIVIRAL DEFENSE, AND SUBCELLULAR LOCATION.
RX PubMed=25126784; DOI=10.1016/j.cell.2014.06.023;
RA Moy R.H., Cole B.S., Yasunaga A., Gold B., Shankarling G., Varble A.,
RA Molleston J.M., tenOever B.R., Lynch K.W., Cherry S.;
RT "Stem-loop recognition by DDX17 facilitates miRNA processing and antiviral
RT defense.";
RL Cell 158:764-777(2014).
RN [42]
RP FUNCTION, AND INTERACTION WITH HNRNPH1.
RX PubMed=24910439; DOI=10.1016/j.celrep.2014.05.010;
RA Dardenne E., Polay Espinoza M., Fattet L., Germann S., Lambert M.P.,
RA Neil H., Zonta E., Mortada H., Gratadou L., Deygas M., Chakrama F.Z.,
RA Samaan S., Desmet F.O., Tranchevent L.C., Dutertre M., Rimokh R.,
RA Bourgeois C.F., Auboeuf D.;
RT "RNA helicases DDX5 and DDX17 dynamically orchestrate transcription, miRNA,
RT and splicing programs in cell differentiation.";
RL Cell Rep. 7:1900-1913(2014).
RN [43]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [44]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-684, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [45]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-129, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [46]
RP FUNCTION, AND MUTAGENESIS OF LYS-221.
RX PubMed=24275493; DOI=10.1093/nar/gkt1216;
RA Samaan S., Tranchevent L.C., Dardenne E., Polay Espinoza M., Zonta E.,
RA Germann S., Gratadou L., Dutertre M., Auboeuf D.;
RT "The Ddx5 and Ddx17 RNA helicases are cornerstones in the complex
RT regulatory array of steroid hormone-signaling pathways.";
RL Nucleic Acids Res. 42:2197-2207(2014).
RN [47]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-129, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [48]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-129, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [49]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-129, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [50]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [51]
RP FUNCTION.
RX PubMed=27478153; DOI=10.1016/j.bbagrm.2016.07.013;
RA Connerty P., Bajan S., Remenyi J., Fuller-Pace F.V., Hutvagner G.;
RT "The miRNA biogenesis factors, p72/DDX17 and KHSRP regulate the protein
RT level of Ago2 in human cells.";
RL Biochim. Biophys. Acta 1859:1299-1305(2016).
RN [52]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-129 AND LYS-528, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: As an RNA helicase, unwinds RNA and alters RNA structures
CC through ATP binding and hydrolysis. Involved in multiple cellular
CC processes, including pre-mRNA splicing, alternative splicing, ribosomal
CC RNA processing and miRNA processing, as well as transcription
CC regulation. Regulates the alternative splicing of exons exhibiting
CC specific features (PubMed:12138182, PubMed:23022728, PubMed:24910439,
CC PubMed:22266867). For instance, promotes the inclusion of AC-rich
CC alternative exons in CD44 transcripts (PubMed:12138182). This function
CC requires the RNA helicase activity (PubMed:12138182, PubMed:23022728,
CC PubMed:24910439, PubMed:22266867). Affects NFAT5 and histone macro-
CC H2A.1/MACROH2A1 alternative splicing in a CDK9-dependent manner
CC (PubMed:26209609, PubMed:22266867). In NFAT5, promotes the introduction
CC of alternative exon 4, which contains 2 stop codons and may target
CC NFAT5 exon 4-containing transcripts to nonsense-mediated mRNA decay,
CC leading to the down-regulation of NFAT5 protein (PubMed:22266867).
CC Affects splicing of mediators of steroid hormone signaling pathway,
CC including kinases that phosphorylates ESR1, such as CDK2, MAPK1 and
CC GSK3B, and transcriptional regulators, such as CREBBP, MED1, NCOR1 and
CC NCOR2. By affecting GSK3B splicing, participates in ESR1 and AR
CC stabilization (PubMed:24275493). In myoblasts and epithelial cells,
CC cooperates with HNRNPH1 to control the splicing of specific subsets of
CC exons (PubMed:24910439). In addition to binding mature mRNAs, also
CC interacts with certain pri-microRNAs, including MIR663/miR-663a,
CC MIR99B/miR-99b, and MIR6087/miR-6087 (PubMed:25126784). Binds pri-
CC microRNAs on the 3' segment flanking the stem loop via the 5'-
CC [ACG]CAUC[ACU]-3' consensus sequence (PubMed:24581491). Required for
CC the production of subsets of microRNAs, including MIR21 and MIR125B1
CC (PubMed:24581491, PubMed:27478153). May be involved not only in
CC microRNA primary transcript processing, but also stabilization (By
CC similarity). Participates in MYC down-regulation at high cell density
CC through the production of MYC-targeting microRNAs (PubMed:24581491).
CC Along with DDX5, may be involved in the processing of the 32S
CC intermediate into the mature 28S ribosomal RNA (PubMed:17485482).
CC Promoter-specific transcription regulator, functioning as a coactivator
CC or corepressor depending on the context of the promoter and the
CC transcriptional complex in which it exists (PubMed:15298701). Enhances
CC NFAT5 transcriptional activity (PubMed:22266867). Synergizes with TP53
CC in the activation of the MDM2 promoter; this activity requires
CC acetylation on lysine residues (PubMed:17226766, PubMed:20663877,
CC PubMed:19995069). May also coactivate MDM2 transcription through a
CC TP53-independent pathway (PubMed:17226766). Coactivates MMP7
CC transcription (PubMed:17226766). Along with CTNNB1, coactivates MYC,
CC JUN, FOSL1 and cyclin D1/CCND1 transcription (PubMed:17699760). Alone
CC or in combination with DDX5 and/or SRA1 non-coding RNA, plays a
CC critical role in promoting the assembly of proteins required for the
CC formation of the transcription initiation complex and chromatin
CC remodeling leading to coactivation of MYOD1-dependent transcription.
CC This helicase-independent activity is required for skeletal muscle
CC cells to properly differentiate into myotubes (PubMed:17011493,
CC PubMed:24910439). During epithelial-to-mesenchymal transition,
CC coregulates SMAD-dependent transcriptional activity, directly
CC controlling key effectors of differentiation, including miRNAs which in
CC turn directly repress its expression (PubMed:24910439). Plays a role in
CC estrogen and testosterone signaling pathway at several levels. Mediates
CC the use of alternative promoters in estrogen-responsive genes and
CC regulates transcription and splicing of a large number of steroid
CC hormone target genes (PubMed:24275493, PubMed:20406972,
CC PubMed:20663877, PubMed:19995069). Contrary to splicing regulation
CC activity, transcriptional coregulation of the estrogen receptor ESR1 is
CC helicase-independent (PubMed:19718048, PubMed:24275493). Plays a role
CC in innate immunity. Specifically restricts bunyavirus infection,
CC including Rift Valley fever virus (RVFV) or La Crosse virus (LACV), but
CC not vesicular stomatitis virus (VSV), in an interferon- and DROSHA-
CC independent manner (PubMed:25126784). Binds to RVFV RNA, likely via
CC structured viral RNA elements (PubMed:25126784). Promotes mRNA
CC degradation mediated by the antiviral zinc-finger protein ZC3HAV1, in
CC an ATPase-dependent manner (PubMed:18334637).
CC {ECO:0000250|UniProtKB:Q501J6, ECO:0000269|PubMed:12138182,
CC ECO:0000269|PubMed:15298701, ECO:0000269|PubMed:17011493,
CC ECO:0000269|PubMed:17226766, ECO:0000269|PubMed:17485482,
CC ECO:0000269|PubMed:17699760, ECO:0000269|PubMed:18334637,
CC ECO:0000269|PubMed:19718048, ECO:0000269|PubMed:19995069,
CC ECO:0000269|PubMed:20406972, ECO:0000269|PubMed:20663877,
CC ECO:0000269|PubMed:22266867, ECO:0000269|PubMed:23022728,
CC ECO:0000269|PubMed:24275493, ECO:0000269|PubMed:24581491,
CC ECO:0000269|PubMed:24910439, ECO:0000269|PubMed:25126784,
CC ECO:0000269|PubMed:26209609, ECO:0000269|PubMed:27478153, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:8871553};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=170 uM for ATP {ECO:0000269|PubMed:8871553};
CC -!- SUBUNIT: Interacts with DDX5 in an RNA-independent manner
CC (PubMed:12595555, PubMed:19995069). Interacts with CDK9 transcription
CC elongation complex under basal conditions. Following cell stimulation
CC with poly(I:C), a synthetic double-stranded RNA mimicking viral
CC infection, the interaction with CDK9 is decreased (PubMed:26209609).
CC Interacts with ESR1 in an estrogen-independent manner (PubMed:19718048,
CC PubMed:20663877). Interacts with HNRNPH1; this interaction is important
CC for the regulation of alternative splicing on G-quadruplex structures
CC (PubMed:24910439). At high, but not low, cell density, interacts with
CC DROSHA and DGCR8, the core components of the microprocessor complex
CC involved in the maturation of primary microRNAs (pri-miRNAs) into pre-
CC miRNAs. The interaction with DGCR8 is reduced during mitosis
CC (PubMed:24589731, PubMed:24581491). At low, but not high, cell density,
CC interacts with YAP1 and with its paralog, WWTR1/TAZ. Interactions with
CC DROSHA and YAP1 are mutually exclusive (PubMed:24581491). In vitro, the
CC pre-miRNA processing activity of the DDX17-containing microprocessor
CC complex is weaker than that of the DROSHA/DGCR8 microprocessor complex
CC devoid of DDX17 (PubMed:15531877). Interacts with UPF3B
CC (PubMed:23788676). Interacts with NFAT5; this interaction leads to
CC DDX17 recruitment to LNC2 and S100A4 promoters and NFAT5-mediated
CC DDX17-enhanced transactivation (PubMed:22266867). Interacts with HDAC1,
CC HDAC2 and HDAC3; this interaction with HDAC1 and HDAC3, but not HDAC2,
CC depends upon DDX17 acetylation (PubMed:15298701, PubMed:20663877).
CC Interacts with ZC3HAV1 (via N-terminal domain) in an RNA-independent
CC manner. Interacts with EXOSC3/RRP40 and EXOSC5/RRP46; this interaction
CC may be indirect and mediated by ZC3HAV1-binding (PubMed:18334637).
CC Interacts with EP300; this interaction leads to acetylation at lysine
CC residues (PubMed:17226766, PubMed:19995069). Interacts with CREBBP/CBP
CC and KAT2B/P/CAF (PubMed:17226766). Directly interacts with CTNNB1
CC (PubMed:17699760). Interacts with MYOD1 (PubMed:17011493). Interacts
CC with TP53 (PubMed:15660129). Interacts with DCP1A in an RNA-independent
CC manner. Interacts with DCP2 in an RNA-dependent manner
CC (PubMed:21876179). Interacts with DHX36; this interaction occurs in a
CC RNA-dependent manner (PubMed:18279852). Interacts with ERCC6
CC (PubMed:26030138). {ECO:0000269|PubMed:12595555,
CC ECO:0000269|PubMed:15298701, ECO:0000269|PubMed:15531877,
CC ECO:0000269|PubMed:15660129, ECO:0000269|PubMed:17011493,
CC ECO:0000269|PubMed:17226766, ECO:0000269|PubMed:17699760,
CC ECO:0000269|PubMed:18279852, ECO:0000269|PubMed:18334637,
CC ECO:0000269|PubMed:19718048, ECO:0000269|PubMed:19995069,
CC ECO:0000269|PubMed:20663877, ECO:0000269|PubMed:21876179,
CC ECO:0000269|PubMed:22266867, ECO:0000269|PubMed:23788676,
CC ECO:0000269|PubMed:24581491, ECO:0000269|PubMed:24589731,
CC ECO:0000269|PubMed:24910439, ECO:0000269|PubMed:26030138,
CC ECO:0000269|PubMed:26209609}.
CC -!- INTERACTION:
CC Q92841; Q13895: BYSL; NbExp=6; IntAct=EBI-746012, EBI-358049;
CC Q92841; P17844: DDX5; NbExp=3; IntAct=EBI-746012, EBI-351962;
CC Q92841; P26196: DDX6; NbExp=3; IntAct=EBI-746012, EBI-351257;
CC Q92841; Q9NQT5: EXOSC3; NbExp=2; IntAct=EBI-746012, EBI-371866;
CC Q92841; O95995: GAS8; NbExp=3; IntAct=EBI-746012, EBI-1052570;
CC Q92841; P62993: GRB2; NbExp=3; IntAct=EBI-746012, EBI-401755;
CC Q92841; P31943: HNRNPH1; NbExp=3; IntAct=EBI-746012, EBI-351590;
CC Q92841; Q8TBB1: LNX1; NbExp=4; IntAct=EBI-746012, EBI-739832;
CC Q92841; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-746012, EBI-14086479;
CC Q92841; O94916: NFAT5; NbExp=3; IntAct=EBI-746012, EBI-308320;
CC Q92841; Q13882: PTK6; NbExp=4; IntAct=EBI-746012, EBI-1383632;
CC Q92841; P98175: RBM10; NbExp=6; IntAct=EBI-746012, EBI-721525;
CC Q92841; Q96T37: RBM15; NbExp=5; IntAct=EBI-746012, EBI-2514922;
CC Q92841; Q15637: SF1; NbExp=4; IntAct=EBI-746012, EBI-744603;
CC Q92841; Q13148: TARDBP; NbExp=6; IntAct=EBI-746012, EBI-372899;
CC Q92841; P04637: TP53; NbExp=3; IntAct=EBI-746012, EBI-366083;
CC Q92841; P46937: YAP1; NbExp=7; IntAct=EBI-746012, EBI-1044059;
CC Q92841; Q9JKL7: Srek1; Xeno; NbExp=3; IntAct=EBI-746012, EBI-6452221;
CC Q92841; Q8K3Y6: Zc3hav1; Xeno; NbExp=6; IntAct=EBI-746012, EBI-8860250;
CC Q92841-4; Q13547: HDAC1; NbExp=3; IntAct=EBI-5280703, EBI-301834;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12138182,
CC ECO:0000269|PubMed:12595555, ECO:0000269|PubMed:17226766,
CC ECO:0000269|PubMed:17699760, ECO:0000269|PubMed:19995069,
CC ECO:0000269|PubMed:22002106, ECO:0000269|PubMed:24581491,
CC ECO:0000269|PubMed:25126784}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:17226766, ECO:0000269|PubMed:22002106}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:25126784}. Note=In the course of bunyavirus
CC infection, relocalizes from the nucleus to the cytosol where it binds
CC viral RNA to antagonize replication. {ECO:0000269|PubMed:25126784}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=1; Synonyms=p82;
CC IsoId=Q92841-4; Sequence=Displayed;
CC Name=2; Synonyms=p72;
CC IsoId=Q92841-1; Sequence=VSP_042527;
CC Name=3;
CC IsoId=Q92841-2; Sequence=VSP_042527, VSP_042528;
CC Name=4;
CC IsoId=Q92841-3; Sequence=VSP_042527, VSP_042529;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:8871553). Low expression,
CC if any, in normal colonic epithelial cells (at protein level). Levels
CC tend to increase during colon cancer progression, from very low in
CC benign hyperplastic polyps to very high in tubular and villous adenomas
CC (PubMed:17699760). {ECO:0000269|PubMed:17699760,
CC ECO:0000269|PubMed:8871553}.
CC -!- PTM: Sumoylation significantly increases stability. It also promotes
CC interaction specifically with HDAC1 (but not HDAC2, nor HDAC3) and
CC strongly stimulates ESR1 and TP53 coactivation.
CC {ECO:0000269|PubMed:19995069}.
CC -!- PTM: Acetylation at lysine residues stabilizes the protein, stimulates
CC interaction with HDAC1 and HDAC3, but not HDAC2, and represses ESR1 and
CC TP53 coactivation activity. {ECO:0000269|PubMed:20663877}.
CC -!- MISCELLANEOUS: [Isoform 1]: Starts at an alternative CUG codon.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-
CC 80 of isoform 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform
CC 2. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform
CC 2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was reported to act as a transcriptional coactivator for
CC estrogen receptor ESR1 (PubMed:11250900). Although this publication was
CC retracted because of aberrations in some figures, this function was
CC also described in other publications by different groups and may be
CC real (PubMed:24275493, PubMed:20406972, PubMed:20663877,
CC PubMed:19995069). {ECO:0000269|PubMed:11250900,
CC ECO:0000269|PubMed:19995069, ECO:0000269|PubMed:20406972,
CC ECO:0000269|PubMed:20663877, ECO:0000269|PubMed:24275493}.
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DR EMBL; U59321; AAC50787.1; -; mRNA.
DR EMBL; CR456432; CAG30318.1; -; mRNA.
DR EMBL; AL713763; CAH10627.2; -; mRNA.
DR EMBL; Z97056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60243.1; -; Genomic_DNA.
DR EMBL; BC000595; AAH00595.2; -; mRNA.
DR CCDS; CCDS33646.1; -. [Q92841-4]
DR PIR; S72367; S72367.
DR RefSeq; NP_006377.2; NM_006386.4. [Q92841-4]
DR PDB; 6UV0; X-ray; 2.60 A; A/B=111-556.
DR PDB; 6UV1; X-ray; 2.31 A; A/B=111-556.
DR PDB; 6UV2; X-ray; 1.89 A; A=111-556.
DR PDB; 6UV3; X-ray; 1.60 A; A=111-556.
DR PDB; 6UV4; X-ray; 1.70 A; A=111-556.
DR PDBsum; 6UV0; -.
DR PDBsum; 6UV1; -.
DR PDBsum; 6UV2; -.
DR PDBsum; 6UV3; -.
DR PDBsum; 6UV4; -.
DR AlphaFoldDB; Q92841; -.
DR SMR; Q92841; -.
DR BioGRID; 115776; 302.
DR CORUM; Q92841; -.
DR DIP; DIP-29843N; -.
DR IntAct; Q92841; 129.
DR MINT; Q92841; -.
DR STRING; 9606.ENSP00000380033; -.
DR BindingDB; Q92841; -.
DR ChEMBL; CHEMBL4105760; -.
DR GlyGen; Q92841; 12 sites, 2 O-linked glycans (12 sites).
DR iPTMnet; Q92841; -.
DR MetOSite; Q92841; -.
DR PhosphoSitePlus; Q92841; -.
DR SwissPalm; Q92841; -.
DR BioMuta; DDX17; -.
DR REPRODUCTION-2DPAGE; IPI00023785; -.
DR CPTAC; CPTAC-351; -.
DR CPTAC; CPTAC-352; -.
DR EPD; Q92841; -.
DR jPOST; Q92841; -.
DR MassIVE; Q92841; -.
DR MaxQB; Q92841; -.
DR PaxDb; Q92841; -.
DR PeptideAtlas; Q92841; -.
DR PRIDE; Q92841; -.
DR ProteomicsDB; 40772; -.
DR ProteomicsDB; 75531; -. [Q92841-4]
DR ProteomicsDB; 75532; -. [Q92841-1]
DR ProteomicsDB; 75533; -. [Q92841-2]
DR ProteomicsDB; 75534; -. [Q92841-3]
DR TopDownProteomics; Q92841-1; -. [Q92841-1]
DR TopDownProteomics; Q92841-4; -. [Q92841-4]
DR Antibodypedia; 26352; 248 antibodies from 29 providers.
DR DNASU; 10521; -.
DR Ensembl; ENST00000403230.3; ENSP00000385536.2; ENSG00000100201.23. [Q92841-4]
DR GeneID; 10521; -.
DR KEGG; hsa:10521; -.
DR MANE-Select; ENST00000403230.3; ENSP00000385536.2; NM_006386.5; NP_006377.2.
DR UCSC; uc062efr.1; human.
DR UCSC; uc062efu.1; human. [Q92841-4]
DR CTD; 10521; -.
DR DisGeNET; 10521; -.
DR GeneCards; DDX17; -.
DR HGNC; HGNC:2740; DDX17.
DR HPA; ENSG00000100201; Low tissue specificity.
DR MIM; 608469; gene.
DR neXtProt; NX_Q92841; -.
DR OpenTargets; ENSG00000100201; -.
DR PharmGKB; PA27206; -.
DR VEuPathDB; HostDB:ENSG00000100201; -.
DR eggNOG; KOG0331; Eukaryota.
DR GeneTree; ENSGT00940000160049; -.
DR HOGENOM; CLU_003041_16_4_1; -.
DR InParanoid; Q92841; -.
DR OMA; VCFPDYC; -.
DR TreeFam; TF300332; -.
DR BRENDA; 3.6.4.13; 2681.
DR PathwayCommons; Q92841; -.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR SignaLink; Q92841; -.
DR SIGNOR; Q92841; -.
DR BioGRID-ORCS; 10521; 88 hits in 1027 CRISPR screens.
DR ChiTaRS; DDX17; human.
DR GeneWiki; DDX17; -.
DR GenomeRNAi; 10521; -.
DR Pharos; Q92841; Tbio.
DR PRO; PR:Q92841; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q92841; protein.
DR Bgee; ENSG00000100201; Expressed in tibia and 202 other tissues.
DR ExpressionAtlas; Q92841; baseline and differential.
DR Genevisible; Q92841; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0010586; P:miRNA metabolic process; IMP:UniProtKB.
DR GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:2001014; P:regulation of skeletal muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd18050; DEADc_DDX17; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR046330; DDX17_ATP-bd-dom.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Alternative splicing;
KW Antiviral defense; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Helicase; Hydrolase; Immunity; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; rRNA processing; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..729
FT /note="Probable ATP-dependent RNA helicase DDX17"
FT /id="PRO_0000054993"
FT DOMAIN 202..377
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 405..552
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 20..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..729
FT /note="Transactivation domain"
FT REGION 551..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..726
FT /note="Interaction with YAP1"
FT /evidence="ECO:0000269|PubMed:24581491"
FT MOTIF 171..199
FT /note="Q motif"
FT MOTIF 325..328
FT /note="DEAD box"
FT COMPBIAS 44..70
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 215..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 108
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000269|PubMed:20663877"
FT MOD_RES 109
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000269|PubMed:20663877"
FT MOD_RES 121
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000269|PubMed:20663877"
FT MOD_RES 523
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 684
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:19995069,
FT ECO:0007744|PubMed:25114211"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 528
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15461802,
FT ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:8871553"
FT /id="VSP_042527"
FT VAR_SEQ 482
FT /note="L -> LGL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_042528"
FT VAR_SEQ 562
FT /note="G -> GKG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15461802"
FT /id="VSP_042529"
FT MUTAGEN 108..109
FT /note="KK->RR: No effect on HDAC1-, HDAC2- nor HDAC3-
FT binding, small decrease in ESR1 coactivation, decreased
FT TP53 coactivation. Complete loss of lysine acetylation,
FT decreased stability, loss of ESR1 and TP53 coactivation and
FT loss of HDAC1- and HDAC3-binding, no effect on HDAC2-
FT binding; when associated with R-121."
FT /evidence="ECO:0000269|PubMed:20663877"
FT MUTAGEN 121
FT /note="K->R: No effect on HDAC1-, HDAC2- nor HDAC3-binding,
FT decreased ESR1 coactivation, strongly decreased TP53
FT coactivation. Complete loss of lysine acetylation,
FT decreased stability, loss of ESR1 and TP53 coactivation and
FT loss of HDAC1- and HDAC3-binding, no effect on HDAC2-
FT binding; when associated with 108-R-R-109."
FT /evidence="ECO:0000269|PubMed:20663877"
FT MUTAGEN 129
FT /note="K->R: Impaired sumoylation and decreased stability.
FT Impairs interaction with HDAC1, but not with HDAC2, nor
FT HDAC3. No effect on EP300-, ESR1-, DDX5- and YAP1-binding."
FT /evidence="ECO:0000269|PubMed:19995069,
FT ECO:0000269|PubMed:24581491"
FT MUTAGEN 221
FT /note="K->N: No effect on transcription activation, when
FT assayed in luciferase reporter gene assays using MDM2 or
FT FOS promoters, either alone or in the presence of EP300 and
FT KAT2B."
FT /evidence="ECO:0000269|PubMed:17226766"
FT MUTAGEN 221
FT /note="K->R: Loss of helicase activity. Loss of splicing
FT regulation in the estrogen signaling pathway. Reduced CD44
FT alternative splicing regulation. Does not promote ZCH3HAV1-
FT mediated RNA degradation."
FT /evidence="ECO:0000269|PubMed:12138182,
FT ECO:0000269|PubMed:18334637, ECO:0000269|PubMed:24275493"
FT MUTAGEN 222
FT /note="T->A: Decreased CD44 alternative splicing."
FT /evidence="ECO:0000269|PubMed:12138182"
FT MUTAGEN 325
FT /note="D->N: Loss of helicase activity. No effect on ESR1
FT coactivation."
FT /evidence="ECO:0000269|PubMed:19718048"
FT MUTAGEN 328
FT /note="D->H: Small decrease in CD44 alternative splicing."
FT /evidence="ECO:0000269|PubMed:12138182"
FT MUTAGEN 355
FT /note="W->G: Small decrease in CD44 alternative splicing."
FT /evidence="ECO:0000269|PubMed:12138182"
FT MUTAGEN 356
FT /note="S->L: Small decrease in CD44 alternative splicing."
FT /evidence="ECO:0000269|PubMed:12138182"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:6UV2"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 221..234
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 254..268
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 284..293
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:6UV3"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 372..380
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 402..414
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 428..440
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 454..466
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 471..474
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 489..494
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 499..506
FT /evidence="ECO:0007829|PDB:6UV3"
FT STRAND 516..522
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 524..529
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 530..539
FT /evidence="ECO:0007829|PDB:6UV3"
FT HELIX 546..551
FT /evidence="ECO:0007829|PDB:6UV3"
SQ SEQUENCE 729 AA; 80272 MW; C819F53515B1BC39 CRC64;
MPTGFVAPIL CVLLPSPTRE AATVASATGD SASERESAAP AAAPTAEAPP PSVVTRPEPQ
ALPSPAIRAP LPDLYPFGTM RGGGFGDRDR DRDRGGFGAR GGGGLPPKKF GNPGERLRKK
KWDLSELPKF EKNFYVEHPE VARLTPYEVD ELRRKKEITV RGGDVCPKPV FAFHHANFPQ
YVMDVLMDQH FTEPTPIQCQ GFPLALSGRD MVGIAQTGSG KTLAYLLPAI VHINHQPYLE
RGDGPICLVL APTRELAQQV QQVADDYGKC SRLKSTCIYG GAPKGPQIRD LERGVEICIA
TPGRLIDFLE SGKTNLRRCT YLVLDEADRM LDMGFEPQIR KIVDQIRPDR QTLMWSATWP
KEVRQLAEDF LRDYTQINVG NLELSANHNI LQIVDVCMES EKDHKLIQLM EEIMAEKENK
TIIFVETKRR CDDLTRRMRR DGWPAMCIHG DKSQPERDWV LNEFRSGKAP ILIATDVASR
GLDVEDVKFV INYDYPNSSE DYVHRIGRTA RSTNKGTAYT FFTPGNLKQA RELIKVLEEA
NQAINPKLMQ LVDHRGGGGG GGGRSRYRTT SSANNPNLMY QDECDRRLRG VKDGGRRDSA
SYRDRSETDR AGYANGSGYG SPNSAFGAQA GQYTYGQGTY GAAAYGTSSY TAQEYGAGTY
GASSTTSTGR SSQSSSQQFS GIGRSGQQPQ PLMSQQFAQP PGATNMIGYM GQTAYQYPPP
PPPPPPSRK
