ID DDX5_HUMAN Reviewed; 614 AA. AC P17844; B4DLW8; B5BU21; D3DU32; E7ETL9; O75681; Q53Y61; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 04-NOV-2026, entry version 256. DE RecName: Full=Probable ATP-dependent RNA helicase DDX5; DE EC=3.6.4.13; DE AltName: Full=DEAD box protein 5; DE AltName: Full=RNA helicase p68; GN Name=DDX5; Synonyms=G17P1, HELR, HLR1; 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 1). RX PubMed=2349099; DOI=10.1093/nar/18.10.3045; RA Hloch P., Stahl H.; RT "Complete cDNA sequence of the human p68 protein."; RL Nucleic Acids Res. 18:3045-3045(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION. RX PubMed=1996094; DOI=10.1128/mcb.11.3.1326-1333.1991; RA Iggo R.D., Jamieson D.J., McNeill S.A., Southgate J., McPheat J., RA Lane D.P.; RT "p68 RNA helicase: identification of a nucleolar form and cloning of RT related genes containing a conserved intron in yeasts."; RL Mol. Cell. Biol. 11:1326-1333(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10648785; DOI=10.1093/nar/28.4.932; RA Roessler O.G., Hloch P., Schutz N., Weitzenegger T., Stahl H.; RT "Structure and expression of the human p68 RNA helicase gene."; RL Nucleic Acids Res. 28:932-939(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [8] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle; 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 [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-614 (ISOFORM 1). RX PubMed=2451786; DOI=10.1038/332736a0; RA Ford M.J., Anton I.A., Lane D.P.; RT "Nuclear protein with sequence homology to translation initiation factor RT eIF-4A."; RL Nature 332:736-738(1988). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-163. RA Petry P., Bammer S., Heinlein U.A.O.; RT "Molecular organization of the murine p68 RNA helicase gene promotor RT region."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [12] RP RETRACTED PAPER. RX PubMed=10409727; DOI=10.1128/mcb.19.8.5363; RA Endoh H., Maruyama K., Masuhiro Y., Kobayashi Y., Goto M., Tai H., RA Yanagisawa J., Metzger D., Hashimoto S., Kato S.; RT "Purification and identification of p68 RNA helicase acting as a RT transcriptional coactivator specific for the activation function 1 of human RT estrogen receptor alpha."; RL Mol. Cell. Biol. 19:5363-5372(1999). RN [13] RP RETRACTION NOTICE OF PUBMED:10409727. RX PubMed=24509260; DOI=10.1128/mcb.01458-13; RA Endoh H., Maruyama K., Masuhiro Y., Kobayashi Y., Goto M., Tai H., RA Yanagisawa J., Metzger D., Hashimoto S., Kato S.; RL Mol. Cell. Biol. 34:915-915(2014). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [15] RP INTERACTION WITH DDX3, SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX PubMed=22034099; DOI=10.1002/jcb.23428; RA Choi Y.J., Lee S.G.; RT "The DEAD-box RNA helicase DDX3 interacts with DDX5, co-localizes with it RT in the cytoplasm during the G2/M phase of the cycle, and affects its RT shuttling during mRNP export."; RL J. Cell. Biochem. 113:985-996(2012). RN [16] RP INTERACTION WITH FBL, AND SUBCELLULAR LOCATION. RX PubMed=10837141; DOI=10.1006/excr.2000.4886; RA Nicol S.M., Causevic M., Prescott A.R., Fuller-Pace F.V.; RT "The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein RT fibrillarin and colocalizes specifically in nascent nucleoli during RT telophase."; RL Exp. Cell Res. 257:272-280(2000). RN [17] RP RETRACTED PAPER. 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 [18] RP 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 [19] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL RP C COMPLEX. RX PubMed=11991638; DOI=10.1017/s1355838202021088; RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.; RT "Purification and characterization of native spliceosomes suitable for RT three-dimensional structural analysis."; RL RNA 8:426-439(2002). RN [20] RP SELF-ASSOCIATION, AND INTERACTION WITH DDX17. 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 [21] RP FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, AND INTERACTION WITH EP300; CREBBP RP AND POLR2A. RX PubMed=12527917; DOI=10.1038/sj.onc.1206067; RA Rossow K.L., Janknecht R.; RT "Synergism between p68 RNA helicase and the transcriptional coactivators RT CBP and p300."; RL Oncogene 22:151-156(2003). RN [22] 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 [23] RP FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, AND 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 [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-297, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [25] RP FUNCTION, INTERACTION WITH MYOD1, AND MUTAGENESIS OF LYS-144. 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 [26] RP INTERACTION WITH AGO1 AND AGO2. RX PubMed=17932509; DOI=10.1038/sj.embor.7401088; RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., RA Urlaub H., Meister G.; RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein RT complexes in human cells."; RL EMBO Rep. 8:1052-1060(2007). RN [27] RP SUMOYLATION AT LYS-53, INTERACTION WITH HDAC1 AND PIAS1, AND MUTAGENESIS OF RP LYS-53 AND GLU-55. RX PubMed=17369852; DOI=10.1038/sj.onc.1210387; RA Jacobs A.M., Nicol S.M., Hislop R.G., Jaffray E.G., Hay R.T., RA Fuller-Pace F.V.; RT "SUMO modification of the DEAD box protein p68 modulates its RT transcriptional activity and promotes its interaction with HDAC1."; RL Oncogene 26:5866-5876(2007). RN [28] RP FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, AND INTERACTION WITH AR. RX PubMed=18829551; DOI=10.1158/0008-5472.can-08-0932; RA Clark E.L., Coulson A., Dalgliesh C., Rajan P., Nicol S.M., Fleming S., RA Heer R., Gaughan L., Leung H.Y., Elliott D.J., Fuller-Pace F.V., RA Robson C.N.; RT "The RNA helicase p68 is a novel androgen receptor coactivator involved in RT splicing and is overexpressed in prostate cancer."; RL Cancer Res. 68:7938-7946(2008). RN [29] 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 [30] RP FUNCTION, AND INTERACTION WITH RUNX2. RX PubMed=17960593; DOI=10.1002/jcb.21526; RA Jensen E.D., Niu L., Caretti G., Nicol S.M., Teplyuk N., Stein G.S., RA Sartorelli V., van Wijnen A.J., Fuller-Pace F.V., Westendorf J.J.; RT "p68 (Ddx5) interacts with Runx2 and regulates osteoblast RT differentiation."; RL J. Cell. Biochem. 103:1438-1451(2008). RN [31] 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 [32] RP FUNCTION, AND INTERACTION WITH ESR1. 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 [33] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-33 AND LYS-40, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [34] RP SUMOYLATION AT LYS-53, MUTAGENESIS OF LYS-53, AND POLYUBIQUITINATION. 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 [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, 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 [36] 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 [37] RP FUNCTION, INTERACTION WITH RBM4, MUTAGENESIS OF ARG-403, AND RNA-BINDING. RX PubMed=21343338; DOI=10.1128/mcb.01149-10; RA Kar A., Fushimi K., Zhou X., Ray P., Shi C., Chen X., Liu Z., Chen S., RA Wu J.Y.; RT "RNA helicase p68 (DDX5) regulates tau exon 10 splicing by modulating a RT stem-loop structure at the 5' splice site."; RL Mol. Cell. Biol. 31:1812-1821(2011). RN [38] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY RP 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 [39] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-480 AND SER-520, AND 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 [40] RP IDENTIFICATION IN RIBONUCLEOPROTEIN COMPLEX, INTERACTION WITH ARVCF, AND RP SUBCELLULAR LOCATION. RX PubMed=24644279; DOI=10.1074/jbc.m113.530717; RA Rappe U., Schlechter T., Aschoff M., Hotz-Wagenblatt A., Hofmann I.; RT "Nuclear ARVCF protein binds splicing factors and contributes to the RT regulation of alternative splicing."; RL J. Biol. Chem. 289:12421-12434(2014). RN [41] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-53, 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 [42] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-53, 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 [43] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-53, 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 [44] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-53, 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 [45] 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 [46] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [47] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-45; LYS-53; LYS-340; RP LYS-343; LYS-388; LYS-391; LYS-411; LYS-437; LYS-451; LYS-470 AND LYS-523, RP AND 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). RN [48] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ADP. RX PubMed=20941364; DOI=10.1371/journal.pone.0012791; RA Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L., Hogbom M., RA Holmberg-Schiavone L., Tempel W., Park H.W., Hammarstrom M., Moche M., RA Thorsell A.G., Schuler H.; RT "Comparative structural analysis of human DEAD-box RNA helicases."; RL PLoS ONE 5:E12791-E12791(2010). CC -!- FUNCTION: Involved in the alternative regulation of pre-mRNA splicing; CC its RNA helicase activity is necessary for increasing tau exon 10 CC inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre- CC mRNA in the stem-loop region downstream of exon 10. The rate of ATP CC hydrolysis is highly stimulated by single-stranded RNA. Involved in CC transcriptional regulation; the function is independent of the RNA CC helicase activity. Transcriptional coactivator for androgen receptor AR CC but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate CC MYOD1 transcriptional activity and involved in skeletal muscle CC differentiation. Transcriptional coactivator for p53/TP53 and involved CC in p53/TP53 transcriptional response to DNA damage and p53/TP53- CC dependent apoptosis. Transcriptional coactivator for RUNX2 and involved CC in regulation of osteoblast differentiation. Acts as a transcriptional CC repressor in a promoter-specific manner; the function probably involves CC association with histone deacetylases, such as HDAC1. As component of a CC large PER complex is involved in the inhibition of 3' transcriptional CC termination of circadian target genes such as PER1 and NR1D1 and the CC control of the circadian rhythms. {ECO:0000269|PubMed:12527917, CC ECO:0000269|PubMed:15298701, ECO:0000269|PubMed:15660129, CC ECO:0000269|PubMed:17011493, ECO:0000269|PubMed:17960593, CC ECO:0000269|PubMed:18829551, ECO:0000269|PubMed:19718048, CC ECO:0000269|PubMed:21343338}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); 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 -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638). CC Component of a ribonucleoprotein complex containing mRNAs and RNA- CC binding proteins including DDX5, HNRNPH2 and SRSF1 as well as splicing CC regulator ARVCF (PubMed:24644279). Interacts with RBM4; the interaction CC occurs in an RNA-independent manner. Interacts with AGO1 and AGO2. CC Interacts with ESR1, AR, EP300, CREBBP, POLR2A, TP53, RUNX2 and HDAC1. CC Self-associates. Interacts with DDX17. Interacts with BRDT. The large CC PER complex involved in the repression of transcriptional termination CC is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A CC (active). Interacts with DHX36; this interaction occurs in a RNA- CC dependent manner (PubMed:18279852). Interacts with NUPR1 (By CC similarity). Interacts with ERCC6 (PubMed:26030138). Interacts with CC DDX3X in the cytoplasm; this interaction may be more efficient when CC both proteins are unphosphorylated (PubMed:22034099). CC {ECO:0000250|UniProtKB:Q61656, ECO:0000269|PubMed:10837141, CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12527917, CC ECO:0000269|PubMed:12595555, ECO:0000269|PubMed:15298701, CC ECO:0000269|PubMed:15660129, ECO:0000269|PubMed:17011493, CC ECO:0000269|PubMed:17369852, ECO:0000269|PubMed:17932509, CC ECO:0000269|PubMed:17960593, ECO:0000269|PubMed:18279852, CC ECO:0000269|PubMed:18829551, ECO:0000269|PubMed:19718048, CC ECO:0000269|PubMed:20941364, ECO:0000269|PubMed:21343338, CC ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:24644279, CC ECO:0000269|PubMed:26030138}. CC -!- INTERACTION: CC P17844; Q12873: CHD3; NbExp=4; IntAct=EBI-351962, EBI-523590; CC P17844; Q92841: DDX17; NbExp=5; IntAct=EBI-351962, EBI-746012; CC P17844; Q9NRR4: DROSHA; NbExp=6; IntAct=EBI-351962, EBI-528367; CC P17844; Q09472: EP300; NbExp=4; IntAct=EBI-351962, EBI-447295; CC P17844; Q01780: EXOSC10; NbExp=3; IntAct=EBI-351962, EBI-358236; CC P17844; P22087: FBL; NbExp=6; IntAct=EBI-351962, EBI-358318; CC P17844; Q13547: HDAC1; NbExp=4; IntAct=EBI-351962, EBI-301834; CC P17844; Q9UI26: IPO11; NbExp=2; IntAct=EBI-351962, EBI-748752; CC P17844; O95983: MBD3; NbExp=4; IntAct=EBI-351962, EBI-1783068; CC P17844; O94916: NFAT5; NbExp=4; IntAct=EBI-351962, EBI-308320; CC P17844; P24928: POLR2A; NbExp=3; IntAct=EBI-351962, EBI-295301; CC P17844; Q15637: SF1; NbExp=3; IntAct=EBI-351962, EBI-744603; CC P17844; Q15797: SMAD1; NbExp=4; IntAct=EBI-351962, EBI-1567153; CC P17844; P84022: SMAD3; NbExp=2; IntAct=EBI-351962, EBI-347161; CC P17844; Q99717: SMAD5; NbExp=3; IntAct=EBI-351962, EBI-6391136; CC P17844; Q13148: TARDBP; NbExp=3; IntAct=EBI-351962, EBI-372899; CC P17844; P04637: TP53; NbExp=6; IntAct=EBI-351962, EBI-366083; CC P17844; P04637-1: TP53; NbExp=2; IntAct=EBI-351962, EBI-3895849; CC P17844; P04637-7: TP53; NbExp=2; IntAct=EBI-351962, EBI-3895873; CC P17844; P45481: Crebbp; Xeno; NbExp=3; IntAct=EBI-351962, EBI-296306; CC P17844; Q8AZK7: EBNA-LP; Xeno; NbExp=2; IntAct=EBI-351962, EBI-1185167; CC P17844; P10085: Myod1; Xeno; NbExp=3; IntAct=EBI-351962, EBI-4405734; CC P17844; Q1K9H5: PB1; Xeno; NbExp=2; IntAct=EBI-351962, EBI-6050669; CC P17844; P04618: rev; Xeno; NbExp=2; IntAct=EBI-351962, EBI-6164309; CC P17844; Q08775-3: Runx2; Xeno; NbExp=2; IntAct=EBI-351962, EBI-6119991; CC P17844; PRO_0000037577 [P27958]; Xeno; NbExp=12; IntAct=EBI-351962, EBI-6904388; CC P17844; PRO_0000308465 [P29991]; Xeno; NbExp=3; IntAct=EBI-351962, EBI-8826747; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22034099}. Nucleus, CC nucleolus {ECO:0000269|PubMed:10837141, ECO:0000269|PubMed:1996094}. CC Nucleus speckle {ECO:0000269|PubMed:24644279}. Cytoplasm CC {ECO:0000269|PubMed:22034099}. Note=During the G0 phase, predominantly CC located in the nucleus. Cytoplasmic levels increase during the G1/S CC phase. During the M phase, located at the vicinity of the condensed CC chromosomes. At G1, localizes in the cytoplasm. CC {ECO:0000269|PubMed:22034099}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P17844-1; Sequence=Displayed; CC Name=2; CC IsoId=P17844-2; Sequence=VSP_056154; CC -!- PTM: Arg-502 is dimethylated, probably to asymmetric dimethylarginine. CC -!- PTM: Sumoylated; sumoylation, promoted by PIAS1, promotes interaction CC with HDAC1 and transcriptional repression activity. Sumoylation also CC significantly increases stability, and reduces polyubiquitination. CC {ECO:0000269|PubMed:17369852, ECO:0000269|PubMed:19995069}. CC -!- PTM: Polyubiquitinated, leading to proteasomal degradation. CC {ECO:0000269|PubMed:19995069}. CC -!- PTM: Weakly phosphorylated in the G1/S phase of the cell cycle and much CC more at G2/M, especially at Thr and Tyr residues. CC {ECO:0000269|PubMed:22034099}. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2 CC subfamily. {ECO:0000305}. CC -!- CAUTION: DDX5 was reported to be a transcriptional coactivator of ESR1. CC However, this study has been retracted due to concerns of image CC manipulation. {ECO:0000305|PubMed:10409727, CC ECO:0000305|PubMed:11250900, ECO:0000305|PubMed:24509260, CC ECO:0000305|PubMed:25452582}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40290/DDX5"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X52104; CAA36324.1; -; mRNA. DR EMBL; AF015812; AAB84094.1; -; Genomic_DNA. DR EMBL; BT006943; AAP35589.1; -; mRNA. DR EMBL; AK297192; BAG59680.1; -; mRNA. DR EMBL; AB451257; BAG70071.1; -; mRNA. DR EMBL; AC009994; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471109; EAW94202.1; -; Genomic_DNA. DR EMBL; CH471109; EAW94203.1; -; Genomic_DNA. DR EMBL; BC016027; AAH16027.1; -; mRNA. DR EMBL; X15729; CAA33751.1; -; mRNA. DR EMBL; AJ010931; CAA09408.1; -; Genomic_DNA. DR CCDS; CCDS11659.1; -. [P17844-1] DR PIR; JC1087; JC1087. DR RefSeq; NP_001307524.1; NM_001320595.2. [P17844-1] DR RefSeq; NP_001307525.1; NM_001320596.3. [P17844-1] DR RefSeq; NP_004387.1; NM_004396.5. [P17844-1] DR PDB; 3FE2; X-ray; 2.60 A; A/B=68-307. DR PDB; 4A4D; X-ray; 2.70 A; A=52-304. DR AlphaFoldDB; P17844; -. DR SMR; P17844; -. DR BioGRID; 108021; 611. DR CORUM; P17844; -. DR DIP; DIP-29844N; -. DR FunCoup; P17844; 3290. DR IntAct; P17844; 253. DR NDEx; IQUERY-CP-DDX5; 5 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000225792; -. DR BindingDB; P17844; -. DR ChEMBL; CHEMBL4295722; -. DR DrugBank; DB11638; Artenimol. DR DrugBank; DB19010; Supinoxin. DR GlyCosmos; P17844; 6 sites, 3 glycans. DR GlyGen; P17844; 7 sites, 1 N-linked glycan (1 site), 2 O-linked glycans (6 sites). DR iPTMnet; P17844; -. DR MetOSite; P17844; -. DR PhosphoSitePlus; P17844; -. DR SwissPalm; P17844; -. DR BioMuta; DDX5; -. DR DMDM; 129383; -. DR jPOST; P17844; -. DR MassIVE; P17844; -. DR PaxDb; 9606-ENSP00000225792; -. DR PeptideAtlas; P17844; -. DR ProteomicsDB; 18237; -. DR ProteomicsDB; 53519; -. [P17844-1] DR Pumba; P17844; -. DR Antibodypedia; 3130; 605 antibodies from 45 providers. DR DNASU; 1655; -. DR Ensembl; ENST00000225792.10; ENSP00000225792.5; ENSG00000108654.17. [P17844-1] DR Ensembl; ENST00000450599.7; ENSP00000403085.3; ENSG00000108654.17. [P17844-1] DR Ensembl; ENST00000577922.6; ENSP00000464337.2; ENSG00000108654.17. [P17844-1] DR Ensembl; ENST00000585111.2; ENSP00000463168.2; ENSG00000108654.17. [P17844-1] DR Ensembl; ENST00000676785.1; ENSP00000504794.1; ENSG00000108654.17. [P17844-1] DR Ensembl; ENST00000874381.1; ENSP00000544440.1; ENSG00000108654.17. [P17844-1] DR Ensembl; ENST00000874384.1; ENSP00000544443.1; ENSG00000108654.17. [P17844-1] DR Ensembl; ENST00000874385.1; ENSP00000544444.1; ENSG00000108654.17. [P17844-1] DR Ensembl; ENST00000874386.1; ENSP00000544445.1; ENSG00000108654.17. [P17844-1] DR Ensembl; ENST00000937089.1; ENSP00000607148.1; ENSG00000108654.17. [P17844-1] DR GeneID; 1655; -. DR KEGG; hsa:1655; -. DR MANE-Select; ENST00000225792.10; ENSP00000225792.5; NM_004396.5; NP_004387.1. DR UCSC; uc002jek.3; human. [P17844-1] DR AGR; HGNC:2746; -. DR ClinPGx; PA27228; -. DR CTD; 1655; -. DR DisGeNET; 1655; -. DR GeneCards; DDX5; -. DR HGNC; HGNC:2746; DDX5. DR HPA; ENSG00000108654; Low tissue specificity. DR MIM; 180630; gene. DR OpenTargets; ENSG00000108654; -. DR VEuPathDB; HostDB:ENSG00000108654; -. DR eggNOG; KOG0331; Eukaryota. DR GeneTree; ENSGT00940000154705; -. DR HOGENOM; CLU_003041_16_4_1; -. DR InParanoid; P17844; -. DR OrthoDB; 196131at2759; -. DR PAN-GO; P17844; 6 GO annotations based on evolutionary models. DR PhylomeDB; P17844; -. DR BRENDA; 5.6.2.6; 2681. DR BRENDA; 5.6.2.7; 2681. DR PathwayCommons; P17844; -. DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR Reactome; R-HSA-9682706; Replication of the SARS-CoV-1 genome. DR Reactome; R-HSA-9694686; Replication of the SARS-CoV-2 genome. DR Reactome; R-HSA-9770562; mRNA Polyadenylation. DR Reactome; R-HSA-9918481; Dengue Virus-Host Interactions. DR SignaLink; P17844; -. DR SIGNOR; P17844; -. DR Agora; ENSG00000108654; -. DR BioGRID-ORCS; 1655; 504 hits in 1166 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; B5B9A610; PML body. DR CD-CODE; C4E5D2FC; Synthetic Condensate 000367. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; DDX5; human. DR EvolutionaryTrace; P17844; -. DR GeneWiki; DDX5; -. DR GenomeRNAi; 1655; -. DR Pharos; P17844; Tbio. DR PRO; PR:P17844; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P17844; protein. DR Bgee; ENSG00000108654; Expressed in calcaneal tendon and 191 other cell types or tissues. DR ExpressionAtlas; P17844; baseline and differential. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl. DR GO; GO:0005516; F:calmodulin binding; IEA:Ensembl. DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl. DR GO; GO:0035500; F:MH2 domain binding; IPI:BHF-UCL. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0050681; F:nuclear androgen receptor binding; IDA:UniProtKB. DR GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB. DR GO; GO:0070878; F:primary miRNA binding; IDA:BHF-UCL. DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB. DR GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL. DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003724; F:RNA helicase activity; IMP:UniProtKB. DR GO; GO:0046332; F:SMAD binding; IPI:BHF-UCL. 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:0030509; P:BMP signaling pathway; IMP:BHF-UCL. DR GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:UniProtKB. DR GO; GO:0030520; P:estrogen receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB. DR GO; GO:0061614; P:miRNA transcription; ISS:UniProtKB. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB. DR GO; GO:0009299; P:mRNA transcription; IMP:CACAO. DR GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IDA:UniProtKB. DR GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB. DR GO; GO:0031053; P:primary miRNA processing; IMP:BHF-UCL. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0045667; P:regulation of osteoblast differentiation; ISS:UniProtKB. DR GO; GO:2001014; P:regulation of skeletal muscle cell differentiation; ISS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0045069; P:regulation of viral genome replication; IEA:Ensembl. DR CDD; cd18049; DEADc_DDX5; 1. DR CDD; cd18787; SF2_C_DEAD; 1. DR FunFam; 3.40.50.300:FF:000008; ATP-dependent RNA helicase RhlB; 1. DR FunFam; 3.40.50.300:FF:000079; probable ATP-dependent RNA helicase DDX17; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C-like. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR012587; P68_rpt. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF08061; P68HR; 2. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM01414; P68HR; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 splicing; ATP-binding; KW Biological rhythms; Cytoplasm; Helicase; Hydrolase; Isopeptide bond; KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; RNA-binding; KW Spliceosome; Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..614 FT /note="Probable ATP-dependent RNA helicase DDX5" FT /id="PRO_0000054991" FT DOMAIN 125..300 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 328..475 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 477..614 FT /note="Transactivation domain" FT REGION 477..504 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 94..122 FT /note="Q motif" FT MOTIF 248..251 FT /note="DEAD box" FT COMPBIAS 1..15 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 488..498 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 114..116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 121 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 138..145 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 32 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 33 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 40 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 236 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q61656" FT MOD_RES 297 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 480 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 520 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 32 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 45 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 53 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT CROSSLNK 53 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 53 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 340 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 343 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 388 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 391 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 411 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 437 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 451 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 470 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 523 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 85..163 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056154" FT VARIANT 480 FT /note="S -> A (in dbSNP:rs1140409)" FT /id="VAR_029241" FT MUTAGEN 53 FT /note="K->R: Abolishes sumoylation, abolishes interaction FT with HDAC1, increases TP53 coactivation and promotes FT polyubiquitination." FT /evidence="ECO:0000269|PubMed:17369852, FT ECO:0000269|PubMed:19995069" FT MUTAGEN 55 FT /note="E->A: Abolishes sumoylation." FT /evidence="ECO:0000269|PubMed:17369852" FT MUTAGEN 144 FT /note="K->R: Abolishes RNA helicase activity." FT /evidence="ECO:0000269|PubMed:17011493" FT MUTAGEN 403 FT /note="R->L: Binds to the tau stem-loop-containing RNA. FT Inhibits tau exon 10 inclusion and RNA cleavage. Does not FT inhibit interaction with RBM4." FT /evidence="ECO:0000269|PubMed:21343338" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:4A4D" FT HELIX 72..80 FT /evidence="ECO:0007829|PDB:3FE2" FT STRAND 82..87 FT /evidence="ECO:0007829|PDB:3FE2" FT HELIX 89..93 FT /evidence="ECO:0007829|PDB:3FE2" FT TURN 96..100 FT /evidence="ECO:0007829|PDB:3FE2" FT HELIX 103..110 FT /evidence="ECO:0007829|PDB:3FE2" FT TURN 111..113 FT /evidence="ECO:0007829|PDB:3FE2" FT HELIX 119..130 FT /evidence="ECO:0007829|PDB:3FE2" FT STRAND 134..138 FT /evidence="ECO:0007829|PDB:3FE2" FT HELIX 144..157 FT /evidence="ECO:0007829|PDB:3FE2" FT HELIX 160..163 FT /evidence="ECO:0007829|PDB:3FE2" FT STRAND 169..173 FT /evidence="ECO:0007829|PDB:3FE2" FT HELIX 177..193 FT /evidence="ECO:0007829|PDB:3FE2" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:3FE2" FT HELIX 207..216 FT /evidence="ECO:0007829|PDB:3FE2" FT STRAND 219..223 FT /evidence="ECO:0007829|PDB:3FE2" FT HELIX 225..234 FT /evidence="ECO:0007829|PDB:3FE2" FT STRAND 239..241 FT /evidence="ECO:0007829|PDB:4A4D" FT STRAND 244..247 FT /evidence="ECO:0007829|PDB:3FE2" FT HELIX 250..255 FT /evidence="ECO:0007829|PDB:3FE2" FT HELIX 259..266 FT /evidence="ECO:0007829|PDB:3FE2" FT STRAND 274..280 FT /evidence="ECO:0007829|PDB:3FE2" FT HELIX 284..293 FT /evidence="ECO:0007829|PDB:3FE2" FT STRAND 298..302 FT /evidence="ECO:0007829|PDB:3FE2" SQ SEQUENCE 614 AA; 69148 MW; 84DF684FD6871594 CRC64; MSGYSSDRDR GRDRGFGAPR FGGSRAGPLS GKKFGNPGEK LVKKKWNLDE LPKFEKNFYQ EHPDLARRTA QEVETYRRSK EITVRGHNCP KPVLNFYEAN FPANVMDVIA RQNFTEPTAI QAQGWPVALS GLDMVGVAQT GSGKTLSYLL PAIVHINHQP FLERGDGPIC LVLAPTRELA QQVQQVAAEY CRACRLKSTC IYGGAPKGPQ IRDLERGVEI CIATPGRLID FLECGKTNLR RTTYLVLDEA DRMLDMGFEP QIRKIVDQIR PDRQTLMWSA TWPKEVRQLA EDFLKDYIHI NIGALELSAN HNILQIVDVC HDVEKDEKLI RLMEEIMSEK ENKTIVFVET KRRCDELTRK MRRDGWPAMG IHGDKSQQER DWVLNEFKHG KAPILIATDV ASRGLDVEDV KFVINYDYPN SSEDYIHRIG RTARSTKTGT AYTFFTPNNI KQVSDLISVL REANQAINPK LLQLVEDRGS GRSRGRGGMK DDRRDRYSAG KRGGFNTFRD RENYDRGYSS LLKRDFGAKT QNGVYSAANY TNGSFGSNFV SAGIQTSFRT GNPTGTYQNG YDSTQQYGSN VPNMHNGMNQ QAYAYPATAA APMIGYPMPT GYSQ //