DDX5_HUMAN
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 03-AUG-2022, entry version 236.
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 (2.6 ANGSTROMS) OF 68-307 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 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 + 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 -!- 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=3; 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; 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="http://atlasgeneticsoncology.org/Genes/DDX5ID40290ch17q23.html";
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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_001320595.1. [P17844-1]
DR RefSeq; NP_001307525.1; NM_001320596.1. [P17844-1]
DR RefSeq; NP_004387.1; NM_004396.4. [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 PDBsum; 3FE2; -.
DR PDBsum; 4A4D; -.
DR AlphaFoldDB; P17844; -.
DR SMR; P17844; -.
DR BioGRID; 108021; 379.
DR CORUM; P17844; -.
DR DIP; DIP-29844N; -.
DR IntAct; P17844; 173.
DR MINT; P17844; -.
DR STRING; 9606.ENSP00000225792; -.
DR ChEMBL; CHEMBL4295722; -.
DR DrugBank; DB11638; Artenimol.
DR GlyGen; P17844; 4 sites, 2 O-linked glycans (4 sites).
DR iPTMnet; P17844; -.
DR MetOSite; P17844; -.
DR PhosphoSitePlus; P17844; -.
DR SwissPalm; P17844; -.
DR BioMuta; DDX5; -.
DR DMDM; 129383; -.
DR SWISS-2DPAGE; P17844; -.
DR EPD; P17844; -.
DR jPOST; P17844; -.
DR MassIVE; P17844; -.
DR MaxQB; P17844; -.
DR PaxDb; P17844; -.
DR PeptideAtlas; P17844; -.
DR PRIDE; P17844; -.
DR ProteomicsDB; 18237; -.
DR ProteomicsDB; 53519; -. [P17844-1]
DR Antibodypedia; 3130; 506 antibodies from 42 providers.
DR DNASU; 1655; -.
DR Ensembl; ENST00000225792.10; ENSP00000225792.5; ENSG00000108654.16. [P17844-1]
DR Ensembl; ENST00000450599.7; ENSP00000403085.3; ENSG00000108654.16. [P17844-1]
DR Ensembl; ENST00000577922.6; ENSP00000464337.2; ENSG00000108654.16. [P17844-1]
DR Ensembl; ENST00000585111.2; ENSP00000463168.2; ENSG00000108654.16. [P17844-1]
DR Ensembl; ENST00000676785.1; ENSP00000504794.1; ENSG00000108654.16. [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 CTD; 1655; -.
DR DisGeNET; 1655; -.
DR GeneCards; DDX5; -.
DR HGNC; HGNC:2746; DDX5.
DR HPA; ENSG00000108654; Low tissue specificity.
DR MIM; 180630; gene.
DR neXtProt; NX_P17844; -.
DR OpenTargets; ENSG00000108654; -.
DR PharmGKB; PA27228; -.
DR VEuPathDB; HostDB:ENSG00000108654; -.
DR eggNOG; KOG0331; Eukaryota.
DR GeneTree; ENSGT00940000154705; -.
DR HOGENOM; CLU_003041_16_4_1; -.
DR InParanoid; P17844; -.
DR OrthoDB; 638613at2759; -.
DR PhylomeDB; P17844; -.
DR TreeFam; TF300332; -.
DR BRENDA; 3.6.4.13; 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 SignaLink; P17844; -.
DR SIGNOR; P17844; -.
DR BioGRID-ORCS; 1655; 483 hits in 1090 CRISPR screens.
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 189 other tissues.
DR ExpressionAtlas; P17844; baseline and differential.
DR Genevisible; P17844; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA: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:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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: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:intracellular 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:1903800; P:positive regulation of miRNA maturation; 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:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
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; IPR012587; P68_rpt.
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 Pfam; PF08061; P68HR; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM01414; P68HR; 2.
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 splicing; ATP-binding;
KW Biological rhythms; Cytoplasm; Helicase; Hydrolase; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Spliceosome;
KW 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..16
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 TURN 96..99
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 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..233
FT /evidence="ECO:0007829|PDB:3FE2"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:4A4D"
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
