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Probable ATP-dependent RNA helicase DDX5 (EC 3.6.4.13) (DEAD box protein 5) (RNA helicase p68)

 DDX5_HUMAN              Reviewed;         614 AA.
P17844; B4DLW8; B5BU21; D3DU32; E7ETL9; O75681; Q53Y61;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
25-OCT-2017, entry version 202.
RecName: Full=Probable ATP-dependent RNA helicase DDX5;
EC=3.6.4.13;
AltName: Full=DEAD box protein 5;
AltName: Full=RNA helicase p68;
Name=DDX5; Synonyms=G17P1, HELR, HLR1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2349099; DOI=10.1093/nar/18.10.3045;
Hloch P., Stahl H.;
"Complete cDNA sequence of the human p68 protein.";
Nucleic Acids Res. 18:3045-3045(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
PubMed=1996094; DOI=10.1128/MCB.11.3.1326;
Iggo R.D., Jamieson D.J., McNeill S.A., Southgate J., McPheat J.,
Lane D.P.;
"p68 RNA helicase: identification of a nucleolar form and cloning of
related genes containing a conserved intron in yeasts.";
Mol. Cell. Biol. 11:1326-1333(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10648785; DOI=10.1093/nar/28.4.932;
Roessler O.G., Hloch P., Schutz N., Weitzenegger T., Stahl H.;
"Structure and expression of the human p68 RNA helicase gene.";
Nucleic Acids Res. 28:932-939(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-614 (ISOFORM 1).
PubMed=2451786; DOI=10.1038/332736a0;
Ford M.J., Anton I.A., Lane D.P.;
"Nuclear protein with sequence homology to translation initiation
factor eIF-4A.";
Nature 332:736-738(1988).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-163.
Petry P., Bammer S., Heinlein U.A.O.;
"Molecular organization of the murine p68 RNA helicase gene promotor
region.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[12]
CAUTION.
PubMed=10409727; DOI=10.1128/MCB.19.8.5363;
Endoh H., Maruyama K., Masuhiro Y., Kobayashi Y., Goto M., Tai H.,
Yanagisawa J., Metzger D., Hashimoto S., Kato S.;
"Purification and identification of p68 RNA helicase acting as a
transcriptional coactivator specific for the activation function 1 of
human estrogen receptor alpha.";
Mol. Cell. Biol. 19:5363-5372(1999).
[13]
ERRATUM, AND RETRACTION.
PubMed=24509260; DOI=10.1128/MCB.01458-13;
Endoh H., Maruyama K., Masuhiro Y., Kobayashi Y., Goto M., Tai H.,
Yanagisawa J., Metzger D., Hashimoto S., Kato S.;
"Retraction: 'Purification and identification of p68 RNA helicase
acting as a transcriptional coactivator specific for the activation
function 1 of human estrogen receptor alpha'.";
Mol. Cell. Biol. 34:915-915(2014).
[14]
INTERACTION WITH FBL, AND SUBCELLULAR LOCATION.
PubMed=10837141; DOI=10.1006/excr.2000.4886;
Nicol S.M., Causevic M., Prescott A.R., Fuller-Pace F.V.;
"The nuclear DEAD box RNA helicase p68 interacts with the nucleolar
protein fibrillarin and colocalizes specifically in nascent nucleoli
during telophase.";
Exp. Cell Res. 257:272-280(2000).
[15]
CAUTION.
PubMed=11250900; DOI=10.1093/emboj/20.6.1341;
Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S.,
Arao Y., Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y.,
Kato S.;
"A subfamily of RNA-binding DEAD-box proteins acts as an estrogen
receptor alpha coactivator through the N-terminal activation domain
(AF-1) with an RNA coactivator, SRA.";
EMBO J. 20:1341-1352(2001).
[16]
ERRATUM, AND RETRACTION.
PubMed=25452582; DOI=10.15252/embj.201470090;
Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S.,
Arao Y., Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y.,
Kato S.;
"Retraction: 'A subfamily of RNA-binding DEAD-box proteins acts as an
estrogen receptor alpha coactivator through the N-terminal activation
domain (AF-1) with an RNA coactivator, SRA'.";
EMBO J. 33:2880-2880(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[18]
SELF-ASSOCIATION, AND INTERACTION WITH DDX17.
PubMed=12595555; DOI=10.1093/nar/gkg236;
Ogilvie V.C., Wilson B.J., Nicol S.M., Morrice N.A., Saunders L.R.,
Barber G.N., Fuller-Pace F.V.;
"The highly related DEAD box RNA helicases p68 and p72 exist as
heterodimers in cells.";
Nucleic Acids Res. 31:1470-1480(2003).
[19]
FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, AND INTERACTION WITH EP300;
CREBBP AND POLR2A.
PubMed=12527917; DOI=10.1038/sj.onc.1206067;
Rossow K.L., Janknecht R.;
"Synergism between p68 RNA helicase and the transcriptional
coactivators CBP and p300.";
Oncogene 22:151-156(2003).
[20]
FUNCTION IN TRANSCRIPTIONAL REPRESSION, AND INTERACTION WITH HDAC1.
PubMed=15298701; DOI=10.1186/1471-2199-5-11;
Wilson B.J., Bates G.J., Nicol S.M., Gregory D.J., Perkins N.D.,
Fuller-Pace F.V.;
"The p68 and p72 DEAD box RNA helicases interact with HDAC1 and
repress transcription in a promoter-specific manner.";
BMC Mol. Biol. 5:11-11(2004).
[21]
FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, AND INTERACTION WITH TP53.
PubMed=15660129; DOI=10.1038/sj.emboj.7600550;
Bates G.J., Nicol S.M., Wilson B.J., Jacobs A.M., Bourdon J.C.,
Wardrop J., Gregory D.J., Lane D.P., Perkins N.D., Fuller-Pace F.V.;
"The DEAD box protein p68: a novel transcriptional coactivator of the
p53 tumour suppressor.";
EMBO J. 24:543-553(2005).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-297, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[23]
FUNCTION, INTERACTION WITH MYOD1, AND MUTAGENESIS OF LYS-144.
PubMed=17011493; DOI=10.1016/j.devcel.2006.08.003;
Caretti G., Schiltz R.L., Dilworth F.J., Di Padova M., Zhao P.,
Ogryzko V., Fuller-Pace F.V., Hoffman E.P., Tapscott S.J.,
Sartorelli V.;
"The RNA helicases p68/p72 and the noncoding RNA SRA are coregulators
of MyoD and skeletal muscle differentiation.";
Dev. Cell 11:547-560(2006).
[24]
INTERACTION WITH AGO1 AND AGO2.
PubMed=17932509; DOI=10.1038/sj.embor.7401088;
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
Urlaub H., Meister G.;
"Proteomic and functional analysis of Argonaute-containing mRNA-
protein complexes in human cells.";
EMBO Rep. 8:1052-1060(2007).
[25]
SUMOYLATION AT LYS-53, INTERACTION WITH HDAC1 AND PIAS1, AND
MUTAGENESIS OF LYS-53 AND GLU-55.
PubMed=17369852; DOI=10.1038/sj.onc.1210387;
Jacobs A.M., Nicol S.M., Hislop R.G., Jaffray E.G., Hay R.T.,
Fuller-Pace F.V.;
"SUMO modification of the DEAD box protein p68 modulates its
transcriptional activity and promotes its interaction with HDAC1.";
Oncogene 26:5866-5876(2007).
[26]
FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, AND INTERACTION WITH AR.
PubMed=18829551; DOI=10.1158/0008-5472.CAN-08-0932;
Clark E.L., Coulson A., Dalgliesh C., Rajan P., Nicol S.M.,
Fleming S., Heer R., Gaughan L., Leung H.Y., Elliott D.J.,
Fuller-Pace F.V., Robson C.N.;
"The RNA helicase p68 is a novel androgen receptor coactivator
involved in splicing and is overexpressed in prostate cancer.";
Cancer Res. 68:7938-7946(2008).
[27]
FUNCTION, AND INTERACTION WITH RUNX2.
PubMed=17960593; DOI=10.1002/jcb.21526;
Jensen E.D., Niu L., Caretti G., Nicol S.M., Teplyuk N., Stein G.S.,
Sartorelli V., van Wijnen A.J., Fuller-Pace F.V., Westendorf J.J.;
"p68 (Ddx5) interacts with Runx2 and regulates osteoblast
differentiation.";
J. Cell. Biochem. 103:1438-1451(2008).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[29]
FUNCTION, AND INTERACTION WITH ESR1.
PubMed=19718048; DOI=10.1038/onc.2009.261;
Wortham N.C., Ahamed E., Nicol S.M., Thomas R.S., Periyasamy M.,
Jiang J., Ochocka A.M., Shousha S., Huson L., Bray S.E., Coombes R.C.,
Ali S., Fuller-Pace F.V.;
"The DEAD-box protein p72 regulates ERalpha-/oestrogen-dependent
transcription and cell growth, and is associated with improved
survival in ERalpha-positive breast cancer.";
Oncogene 28:4053-4064(2009).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-33 AND LYS-40, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[31]
SUMOYLATION AT LYS-53, MUTAGENESIS OF LYS-53, AND POLYUBIQUITINATION.
PubMed=19995069; DOI=10.1021/bi901263m;
Mooney S.M., Grande J.P., Salisbury J.L., Janknecht R.;
"Sumoylation of p68 and p72 RNA helicases affects protein stability
and transactivation potential.";
Biochemistry 49:1-10(2010).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[34]
FUNCTION, INTERACTION WITH RBM4, MUTAGENESIS OF ARG-403, AND
RNA-BINDING.
PubMed=21343338; DOI=10.1128/MCB.01149-10;
Kar A., Fushimi K., Zhou X., Ray P., Shi C., Chen X., Liu Z., Chen S.,
Wu J.Y.;
"RNA helicase p68 (DDX5) regulates tau exon 10 splicing by modulating
a stem-loop structure at the 5' splice site.";
Mol. Cell. Biol. 31:1812-1821(2011).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-480 AND SER-520,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[37]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[39]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[40]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[41]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[42]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-45; LYS-53; LYS-340;
LYS-343; LYS-388; LYS-391; LYS-411; LYS-437; LYS-451; LYS-470 AND
LYS-523, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[43]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 68-307 IN COMPLEX WITH ADP.
PubMed=20941364; DOI=10.1371/journal.pone.0012791;
Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L.,
Hogbom M., Holmberg-Schiavone L., Tempel W., Park H.W.,
Hammarstrom M., Moche M., Thorsell A.G., Schuler H.;
"Comparative structural analysis of human DEAD-box RNA helicases.";
PLoS ONE 5:E12791-E12791(2010).
-!- FUNCTION: Involved in the alternative regulation of pre-mRNA
splicing; its RNA helicase activity is necessary for increasing
tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds
to the tau pre-mRNA in the stem-loop region downstream of exon 10.
The rate of ATP hydrolysis is highly stimulated by single-stranded
RNA. Involved in transcriptional regulation; the function is
independent of the RNA helicase activity. Transcriptional
coactivator for androgen receptor AR but probably not ESR1.
Synergizes with DDX17 and SRA1 RNA to activate MYOD1
transcriptional activity and involved in skeletal muscle
differentiation. Transcriptional coactivator for p53/TP53 and
involved in p53/TP53 transcriptional response to DNA damage and
p53/TP53-dependent apoptosis. Transcriptional coactivator for
RUNX2 and involved in regulation of osteoblast differentiation.
Acts as transcriptional repressor in a promoter-specific manner;
the function probably involves association with histone
deacetylases, such as HDAC1. As component of a large PER complex
is involved in the inhibition of 3' transcriptional termination of
circadian target genes such as PER1 and NR1D1 and the control of
the circadian rhythms. {ECO:0000269|PubMed:12527917,
ECO:0000269|PubMed:15298701, ECO:0000269|PubMed:15660129,
ECO:0000269|PubMed:17011493, ECO:0000269|PubMed:17960593,
ECO:0000269|PubMed:18829551, ECO:0000269|PubMed:19718048,
ECO:0000269|PubMed:21343338}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Identified in the spliceosome C complex. Interacts with
RBM4; the interaction occurs in an RNA-independent manner.
Interacts with AGO1 and AGO2. Interacts with ESR1, AR, EP300,
CREBBP, POLR2A, TP53, RUNX2 and HDAC1. Self-associates. Interacts
with DDX17. Interacts with BRDT. The large PER complex involved in
the repression of transcriptional termination is composed of at
least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active).
{ECO:0000269|PubMed:10837141, ECO:0000269|PubMed:11991638,
ECO:0000269|PubMed:12527917, ECO:0000269|PubMed:12595555,
ECO:0000269|PubMed:15298701, ECO:0000269|PubMed:15660129,
ECO:0000269|PubMed:17011493, ECO:0000269|PubMed:17369852,
ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:17960593,
ECO:0000269|PubMed:18829551, ECO:0000269|PubMed:19718048,
ECO:0000269|PubMed:20941364, ECO:0000269|PubMed:21343338}.
-!- INTERACTION:
P27958:- (xeno); NbExp=12; IntAct=EBI-351962, EBI-6904388;
P29991:- (xeno); NbExp=3; IntAct=EBI-351962, EBI-8826747;
Q12873:CHD3; NbExp=4; IntAct=EBI-351962, EBI-523590;
P45481:Crebbp (xeno); NbExp=3; IntAct=EBI-351962, EBI-296306;
Q92841:DDX17; NbExp=3; IntAct=EBI-351962, EBI-746012;
Q9NRR4:DROSHA; NbExp=6; IntAct=EBI-351962, EBI-528367;
Q8AZK7:EBNA-LP (xeno); NbExp=2; IntAct=EBI-351962, EBI-1185167;
Q09472:EP300; NbExp=4; IntAct=EBI-351962, EBI-447295;
P03372:ESR1; NbExp=9; IntAct=EBI-351962, EBI-78473;
Q01780:EXOSC10; NbExp=3; IntAct=EBI-351962, EBI-358236;
P22087:FBL; NbExp=6; IntAct=EBI-351962, EBI-358318;
Q13547:HDAC1; NbExp=4; IntAct=EBI-351962, EBI-301834;
O95983:MBD3; NbExp=4; IntAct=EBI-351962, EBI-1783068;
P10085:Myod1 (xeno); NbExp=3; IntAct=EBI-351962, EBI-4405734;
O94916:NFAT5; NbExp=4; IntAct=EBI-351962, EBI-308320;
Q1K9H5:PB1 (xeno); NbExp=2; IntAct=EBI-351962, EBI-6050669;
P24928:POLR2A; NbExp=3; IntAct=EBI-351962, EBI-295301;
P04618:rev (xeno); NbExp=2; IntAct=EBI-351962, EBI-6164309;
Q08775-3:Runx2 (xeno); NbExp=2; IntAct=EBI-351962, EBI-6119991;
Q15637:SF1; NbExp=3; IntAct=EBI-351962, EBI-744603;
Q15797:SMAD1; NbExp=4; IntAct=EBI-351962, EBI-1567153;
P84022:SMAD3; NbExp=2; IntAct=EBI-351962, EBI-347161;
Q99717:SMAD5; NbExp=3; IntAct=EBI-351962, EBI-6391136;
P04637:TP53; NbExp=6; IntAct=EBI-351962, EBI-366083;
P04637-1:TP53; NbExp=2; IntAct=EBI-351962, EBI-3895849;
P04637-7:TP53; NbExp=2; IntAct=EBI-351962, EBI-3895873;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:10837141, ECO:0000269|PubMed:1996094}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P17844-1; Sequence=Displayed;
Name=2;
IsoId=P17844-2; Sequence=VSP_056154;
Note=No experimental confirmation available.;
-!- PTM: Arg-502 is dimethylated, probably to asymmetric
dimethylarginine.
-!- PTM: Sumoylated; sumoylation, promoted by PIAS1, promotes
interaction with HDAC1 and transcriptional repression activity.
Sumoylation also significantly increases stability, and reduces
polyubiquitination. {ECO:0000269|PubMed:17369852,
ECO:0000269|PubMed:19995069}.
-!- PTM: Polyubiquitinated, leading to proteasomal degradation.
{ECO:0000269|PubMed:19995069}.
-!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2
subfamily. {ECO:0000305}.
-!- CAUTION: Was reported to act as transcriptional coactivator for
estrogen receptor ESR1; these publications have been retracted
(PubMed:10409727, PubMed:11250900). The function has been
questioned (PubMed:18829551). {ECO:0000269|PubMed:10409727,
ECO:0000269|PubMed:11250900, ECO:0000269|PubMed:18829551}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DDX5ID40290ch17q23.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X52104; CAA36324.1; -; mRNA.
EMBL; AF015812; AAB84094.1; -; Genomic_DNA.
EMBL; BT006943; AAP35589.1; -; mRNA.
EMBL; AK297192; BAG59680.1; -; mRNA.
EMBL; AB451257; BAG70071.1; -; mRNA.
EMBL; AC009994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94202.1; -; Genomic_DNA.
EMBL; CH471109; EAW94203.1; -; Genomic_DNA.
EMBL; BC016027; AAH16027.1; -; mRNA.
EMBL; X15729; CAA33751.1; -; mRNA.
EMBL; AJ010931; CAA09408.1; -; Genomic_DNA.
CCDS; CCDS11659.1; -. [P17844-1]
PIR; JC1087; JC1087.
RefSeq; NP_001307524.1; NM_001320595.1. [P17844-1]
RefSeq; NP_001307525.1; NM_001320596.1. [P17844-1]
RefSeq; NP_004387.1; NM_004396.4. [P17844-1]
UniGene; Hs.279806; -.
PDB; 3FE2; X-ray; 2.60 A; A/B=68-307.
PDB; 4A4D; X-ray; 2.70 A; A=52-304.
PDBsum; 3FE2; -.
PDBsum; 4A4D; -.
ProteinModelPortal; P17844; -.
SMR; P17844; -.
BioGrid; 108021; 226.
CORUM; P17844; -.
DIP; DIP-29844N; -.
IntAct; P17844; 128.
MINT; MINT-5000516; -.
STRING; 9606.ENSP00000225792; -.
iPTMnet; P17844; -.
PhosphoSitePlus; P17844; -.
SwissPalm; P17844; -.
BioMuta; DDX5; -.
DMDM; 129383; -.
SWISS-2DPAGE; P17844; -.
EPD; P17844; -.
MaxQB; P17844; -.
PaxDb; P17844; -.
PeptideAtlas; P17844; -.
PRIDE; P17844; -.
DNASU; 1655; -.
Ensembl; ENST00000225792; ENSP00000225792; ENSG00000108654. [P17844-1]
Ensembl; ENST00000450599; ENSP00000403085; ENSG00000108654. [P17844-2]
GeneID; 1655; -.
KEGG; hsa:1655; -.
UCSC; uc002jek.3; human. [P17844-1]
CTD; 1655; -.
DisGeNET; 1655; -.
EuPathDB; HostDB:ENSG00000108654.11; -.
GeneCards; DDX5; -.
HGNC; HGNC:2746; DDX5.
HPA; CAB005868; -.
HPA; HPA020043; -.
MIM; 180630; gene.
neXtProt; NX_P17844; -.
OpenTargets; ENSG00000108654; -.
PharmGKB; PA27228; -.
eggNOG; KOG0331; Eukaryota.
eggNOG; COG0513; LUCA.
GeneTree; ENSGT00900000140856; -.
HOGENOM; HOG000268804; -.
HOVERGEN; HBG015893; -.
InParanoid; P17844; -.
KO; K12823; -.
PhylomeDB; P17844; -.
TreeFam; TF300332; -.
BRENDA; 3.6.4.13; 2681.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
SIGNOR; P17844; -.
ChiTaRS; DDX5; human.
EvolutionaryTrace; P17844; -.
GeneWiki; DDX5; -.
GenomeRNAi; 1655; -.
PRO; PR:P17844; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108654; -.
CleanEx; HS_DDX5; -.
ExpressionAtlas; P17844; baseline and differential.
Genevisible; P17844; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0050681; F:androgen receptor binding; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central.
GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0035500; F:MH2 domain binding; IPI:BHF-UCL.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB.
GO; GO:0070878; F:primary miRNA binding; IDA:BHF-UCL.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003724; F:RNA helicase activity; IMP:UniProtKB.
GO; GO:0046332; F:SMAD binding; IPI:BHF-UCL.
GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; IMP:UniProtKB.
GO; GO:0030509; P:BMP signaling pathway; IMP:BHF-UCL.
GO; GO:0016049; P:cell growth; NAS:UniProtKB.
GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:UniProtKB.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IMP:UniProtKB.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0009299; P:mRNA transcription; IMP:CACAO.
GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IDA:UniProtKB.
GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; IMP:BHF-UCL.
GO; GO:0061614; P:pri-miRNA transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IMP:UniProtKB.
GO; GO:0045667; P:regulation of osteoblast differentiation; ISS:UniProtKB.
GO; GO:2001014; P:regulation of skeletal muscle cell differentiation; ISS:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0045069; P:regulation of viral genome replication; IEA:Ensembl.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central.
CDD; cd00079; HELICc; 1.
InterPro; IPR033488; DDX5.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR012587; P68_rpt.
InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
PANTHER; PTHR24031:SF404; PTHR24031:SF404; 1.
Pfam; PF00270; DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF08061; P68HR; 2.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM01414; P68HR; 2.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51195; Q_MOTIF; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Biological rhythms; Complete proteome; Helicase; Hydrolase;
Isopeptide bond; mRNA processing; mRNA splicing; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
RNA-binding; Spliceosome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 614 Probable ATP-dependent RNA helicase DDX5.
/FTId=PRO_0000054991.
DOMAIN 125 300 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 328 475 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 114 116 ATP.
NP_BIND 138 145 ATP.
REGION 477 614 Transactivation domain.
MOTIF 94 122 Q motif.
MOTIF 248 251 DEAD box.
BINDING 121 121 ATP.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 32 32 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 33 33 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 40 40 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 236 236 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q61656}.
MOD_RES 297 297 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 480 480 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 520 520 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 45 45 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 53 53 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 53 53 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 53 53 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 340 340 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 343 343 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 388 388 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 391 391 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 411 411 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 437 437 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 451 451 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 470 470 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 523 523 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 85 163 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056154.
VARIANT 480 480 S -> A (in dbSNP:rs1140409).
/FTId=VAR_029241.
MUTAGEN 53 53 K->R: Abolishes sumoylation, abolishes
interaction with HDAC1, increases TP53
coactivation and promotes
polyubiquitination.
{ECO:0000269|PubMed:17369852,
ECO:0000269|PubMed:19995069}.
MUTAGEN 55 55 E->A: Abolishes sumoylation.
{ECO:0000269|PubMed:17369852}.
MUTAGEN 144 144 K->R: Abolishes RNA helicase activity.
{ECO:0000269|PubMed:17011493}.
MUTAGEN 403 403 R->L: Binds to the tau stem-loop-
containing RNA. Inhibits tau exon 10
inclusion and RNA cleavage. Does not
inhibit interaction with RBM4.
{ECO:0000269|PubMed:21343338}.
HELIX 64 66 {ECO:0000244|PDB:4A4D}.
HELIX 72 80 {ECO:0000244|PDB:3FE2}.
STRAND 82 87 {ECO:0000244|PDB:3FE2}.
TURN 96 99 {ECO:0000244|PDB:3FE2}.
HELIX 103 110 {ECO:0000244|PDB:3FE2}.
TURN 111 113 {ECO:0000244|PDB:3FE2}.
HELIX 119 130 {ECO:0000244|PDB:3FE2}.
STRAND 134 138 {ECO:0000244|PDB:3FE2}.
HELIX 144 157 {ECO:0000244|PDB:3FE2}.
STRAND 169 173 {ECO:0000244|PDB:3FE2}.
HELIX 177 193 {ECO:0000244|PDB:3FE2}.
STRAND 198 201 {ECO:0000244|PDB:3FE2}.
HELIX 207 216 {ECO:0000244|PDB:3FE2}.
STRAND 219 223 {ECO:0000244|PDB:3FE2}.
HELIX 225 233 {ECO:0000244|PDB:3FE2}.
TURN 234 236 {ECO:0000244|PDB:4A4D}.
STRAND 239 241 {ECO:0000244|PDB:4A4D}.
STRAND 244 247 {ECO:0000244|PDB:3FE2}.
HELIX 250 255 {ECO:0000244|PDB:3FE2}.
HELIX 259 266 {ECO:0000244|PDB:3FE2}.
STRAND 274 280 {ECO:0000244|PDB:3FE2}.
HELIX 284 293 {ECO:0000244|PDB:3FE2}.
STRAND 298 302 {ECO:0000244|PDB:3FE2}.
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


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EIAAB10794 ATP-dependent RNA helicase DDX42,DDX42,DEAD box protein 42,Homo sapiens,Human,RHELP,RNA helicase-like protein,RNA helicase-related protein,RNAHP,SF3b DEAD box protein,SF3b125,Splicing factor 3B-associ
EIAAB10797 Ddx46,DEAD box protein 46,Hel117,Helicase of 117.4 kDa,Probable ATP-dependent RNA helicase DDX46,Rat,Rattus norvegicus
EIAAB10813 ATP-dependent RNA helicase ROK1-like,DDX52,DEAD box protein 52,Homo sapiens,Human,HUSSY-19,Probable ATP-dependent RNA helicase DDX52,ROK1
EIAAB10814 ATP-dependent RNA helicase ROK1-like,Ddx52,DEAD box protein 52,Probable ATP-dependent RNA helicase DDX52,Rat,Rattus norvegicus,Rok1,rROK1L
EIAAB10812 ATP-dependent RNA helicase ROK1-like,Ddx52,DEAD box protein 52,Mouse,Mus musculus,Probable ATP-dependent RNA helicase DDX52,Rok1
CSB-EL006630HU Human Probable ATP-dependent RNA helicase DDX5(DDX5) ELISA kit SpeciesHuman 96T
CSB-EL006630MO Mouse Probable ATP-dependent RNA helicase DDX5(DDX5) ELISA kit SpeciesMouse 96T
G0992 Probable ATP-dependent RNA helicase DDX5 (DDX5), Mouse, ELISA Kit 96T
G0991 Probable ATP-dependent RNA helicase DDX5 (DDX5), Human, ELISA Kit 96T
CSB-EL006630HU Human Probable ATP-dependent RNA helicase DDX5(DDX5) ELISA kit 96T
CSB-EL006630MO Mouse Probable ATP-dependent RNA helicase DDX5(DDX5) ELISA kit 96T
DDX5_MOUSE ELISA Kit FOR Probable ATP-dependent RNA helicase DDX5; organism: Mouse; gene name: Ddx5 96T
25-214 SMARCAD1 belongs to the SNF2_RAD54 helicase family. It contains 2 CUE domains, 1 helicase ATP-binding domain, and 1 helicase C-terminal domain. It is a probable ATP-dependent DNA helicase. 0.05 mg
EIAAB10783 ATP-dependent RNA helicase DDX3X,D1Pas1-related sequence 2,D1Pas1-rs2,Ddx3,Ddx3x,DEAD box protein 3, X-chromosomal,DEAD box RNA helicase DEAD3,Dead3,Embryonic RNA helicase,Erh,mDEAD3,Mouse,Mus musculu


 

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