GENTAUR Molecular Products.

 DDX20_HUMAN             Reviewed;         824 AA.
 Q9UHI6; B4DWV7; Q96F72; Q9NVM3; Q9UF59; Q9UIY0; Q9Y659;
 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
 01-DEC-2000, sequence version 2.
 28-MAR-2018, entry version 195.
 RecName: Full=Probable ATP-dependent RNA helicase DDX20;
          EC=3.6.4.13;
 AltName: Full=Component of gems 3;
 AltName: Full=DEAD box protein 20;
 AltName: Full=DEAD box protein DP 103;
 AltName: Full=Gemin-3;
 Name=DDX20; Synonyms=DP103, GEMIN3;
 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), IDENTIFICATION IN THE CORE SMN
 COMPLEX, INTERACTION WITH SNRPB; SNRPD2 AND SNRPD3, AND IDENTIFICATION
 BY MASS SPECTROMETRY.
 PubMed=10601333; DOI=10.1083/jcb.147.6.1181;
 Charroux B., Pellizzoni L., Perkinson R.A., Shevchenko A., Mann M.,
 Dreyfuss G.;
 "Gemin3: a novel DEAD box protein that interacts with SMN, the spinal
 muscular atrophy gene product, and a component of gems.";
 J. Cell Biol. 147:1181-1194(1999).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH EBV EBNA2
 AND EBV EBNA3C.
 PubMed=10383418; DOI=10.1074/jbc.274.27.19136;
 Grundhoff A.T., Kremmer E., Tuereci O., Glieden A., Gindorf C.,
 Atz J., Mueller-Lantzsch N., Schubach W.H., Grasser F.A.;
 "Characterization of DP103, a novel DEAD box protein that binds to the
 Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C.";
 J. Biol. Chem. 274:19136-19144(1999).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
 TISSUE=Esophagus;
 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).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=16710414; DOI=10.1038/nature04727;
 Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
 Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
 Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
 McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
 Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
 Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
 Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
 Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
 Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
 Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
 Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
 Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
 Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
 Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
 Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
 Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
 Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
 Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
 Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
 Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
 Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
 Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
 Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
 Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
 Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
 Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
 Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
 Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
 Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
 Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
 Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
 Beck S., Rogers J., Bentley D.R.;
 "The DNA sequence and biological annotation of human chromosome 1.";
 Nature 441:315-321(2006).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
 THR-636.
 TISSUE=Placenta;
 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).
 [6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-275 (ISOFORM 1).
 TISSUE=Testis;
 PubMed=17974005; DOI=10.1186/1471-2164-8-399;
 Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
 Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
 Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
 Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
 "The full-ORF clone resource of the German cDNA consortium.";
 BMC Genomics 8:399-399(2007).
 [7]
 INTERACTION WITH SNUPN; SMN1 AND SNRPB.
 PubMed=12095920; DOI=10.1093/hmg/11.15.1785;
 Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.;
 "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP
 complex with snurportin1 and importin beta.";
 Hum. Mol. Genet. 11:1785-1795(2002).
 [8]
 INTERACTION WITH PPP4R2.
 PubMed=12668731; DOI=10.1242/jcs.00409;
 Carnegie G.K., Sleeman J.E., Morrice N., Hastie C.J., Peggie M.W.,
 Philp A., Lamond A.I., Cohen P.T.W.;
 "Protein phosphatase 4 interacts with the survival of motor neurons
 complex and enhances the temporal localisation of snRNPs.";
 J. Cell Sci. 116:1905-1913(2003).
 [9]
 INTERACTION WITH FOXL2.
 PubMed=16153597; DOI=10.1016/j.bbrc.2005.08.184;
 Lee K., Pisarska M.D., Ko J.J., Kang Y., Yoon S., Ryou S.M., Cha K.Y.,
 Bae J.;
 "Transcriptional factor FOXL2 interacts with DP103 and induces
 apoptosis.";
 Biochem. Biophys. Res. Commun. 336:876-881(2005).
 [10]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-688, AND IDENTIFICATION
 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=16964243; DOI=10.1038/nbt1240;
 Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
 "A probability-based approach for high-throughput protein
 phosphorylation analysis and site localization.";
 Nat. Biotechnol. 24:1285-1292(2006).
 [11]
 FUNCTION IN SNRNP BIOGENESIS, AND IDENTIFICATION IN SMN-SM COMPLEX.
 PubMed=18984161; DOI=10.1016/j.cell.2008.09.020;
 Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B.,
 Englbrecht C., Sickmann A., Stark H., Fischer U.;
 "An assembly chaperone collaborates with the SMN complex to generate
 spliceosomal SnRNPs.";
 Cell 135:497-509(2008).
 [12]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; THR-552 AND
 SER-714, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
 ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
 Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
 Greff Z., Keri G., Stemmann O., Mann M.;
 "Kinase-selective enrichment enables quantitative phosphoproteomics of
 the kinome across the cell cycle.";
 Mol. Cell 31:438-448(2008).
 [13]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-500; SER-532;
 THR-552; SER-652; SER-654; SER-656; SER-677; SER-678; SER-703; THR-705
 AND SER-714, AND 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).
 [14]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=19413330; DOI=10.1021/ac9004309;
 Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
 Mohammed S.;
 "Lys-N and trypsin cover complementary parts of the phosphoproteome in
 a refined SCX-based approach.";
 Anal. Chem. 81:4493-4501(2009).
 [15]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677; SER-678 AND
 SER-703, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
 ANALYSIS].
 TISSUE=Leukemic T-cell;
 PubMed=19690332; DOI=10.1126/scisignal.2000007;
 Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
 Rodionov V., Han D.K.;
 "Quantitative phosphoproteomic analysis of T cell receptor signaling
 reveals system-wide modulation of protein-protein interactions.";
 Sci. Signal. 2:RA46-RA46(2009).
 [16]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672; SER-678 AND
 SER-714, 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).
 [17]
 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).
 [18]
 INTERACTION WITH PUM2 AND NANOS1.
 PubMed=21800163; DOI=10.1007/s00418-011-0842-y;
 Ginter-Matuszewska B., Kusz K., Spik A., Grzeszkowiak D.,
 Rembiszewska A., Kupryjanczyk J., Jaruzelska J.;
 "NANOS1 and PUMILIO2 bind microRNA biogenesis factor GEMIN3, within
 chromatoid body in human germ cells.";
 Histochem. Cell Biol. 136:279-287(2011).
 [19]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505; SER-672; SER-677
 AND SER-678, 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).
 [20]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268; SER-269; SER-505;
 THR-552; SER-560; SER-672; SER-677; SER-678; SER-703; THR-705 AND
 SER-714, 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).
 [21]
 X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 41-268 IN COMPLEX WITH ADP,
 AND ADP-BINDING.
 PubMed=20510246; DOI=10.1016/j.jmb.2010.05.046;
 Schutz P., Wahlberg E., Karlberg T., Hammarstrom M., Collins R.,
 Flores A., Schuler H.;
 "Crystal structure of human RNA helicase A (DHX9): structural basis
 for unselective nucleotide base binding in a DEAD-box variant
 protein.";
 J. Mol. Biol. 400:768-782(2010).
 [22]
 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 41-268.
 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: The SMN complex plays a catalyst role in the assembly of
     small nuclear ribonucleoproteins (snRNPs), the building blocks of
     the spliceosome. Thereby, plays an important role in the splicing
     of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common
     set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and
     SNRPG that assemble in a heptameric protein ring on the Sm site of
     the small nuclear RNA to form the core snRNP. In the cytosol, the
     Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in
     an inactive 6S pICln-Sm complex by the chaperone CLNS1A that
     controls the assembly of the core snRNP. Dissociation by the SMN
     complex of CLNS1A from the trapped Sm proteins and their transfer
     to an SMN-Sm complex triggers the assembly of core snRNPs and
     their transport to the nucleus. May also play a role in the
     metabolism of small nucleolar ribonucleoprotein (snoRNPs).
     {ECO:0000269|PubMed:18984161}.
 -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
 -!- SUBUNIT: Part of the core SMN complex that contains SMN1,
     GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8
     and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1,
     GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8,
     STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3,
     SNRPE, SNRPF and SNRPG. Interacts directly with GEMIN5. Interacts
     directly with SNUPN. Interacts with PPP4R2. Interacts with FOXL2.
     Interacts with EBV EBNA2 and EBNA3C. Interacts with NANOS1 and
     PUM2. {ECO:0000269|PubMed:10383418, ECO:0000269|PubMed:10601333,
     ECO:0000269|PubMed:12095920, ECO:0000269|PubMed:12668731,
     ECO:0000269|PubMed:16153597, ECO:0000269|PubMed:18984161,
     ECO:0000269|PubMed:20510246, ECO:0000269|PubMed:21800163}.
 -!- INTERACTION:
     P57678:GEMIN4; NbExp=8; IntAct=EBI-347658, EBI-356700;
     P01106:MYC; NbExp=2; IntAct=EBI-347658, EBI-447544;
 -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, gem. Note=Localized in
     subnuclear structures next to coiled bodies, called Gemini of
     Cajal bodies (Gems).
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=2;
     Name=1;
       IsoId=Q9UHI6-1; Sequence=Displayed;
     Name=2;
       IsoId=Q9UHI6-2; Sequence=VSP_056505, VSP_056506;
       Note=No experimental confirmation available.;
 -!- TISSUE SPECIFICITY: Ubiquitous.
 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX20
     subfamily. {ECO:0000305}.
 -----------------------------------------------------------------------
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 EMBL; AF171063; AAF14544.1; -; mRNA.
 EMBL; AF106019; AAD42744.1; -; mRNA.
 EMBL; AK001506; BAA91727.1; -; mRNA.
 EMBL; AK301697; BAG63169.1; -; mRNA.
 EMBL; AL049557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; BC011556; AAH11556.1; -; mRNA.
 EMBL; AL133598; CAB63734.2; -; mRNA.
 CCDS; CCDS842.1; -. [Q9UHI6-1]
 PIR; T43476; T43476.
 RefSeq; NP_009135.4; NM_007204.4. [Q9UHI6-1]
 UniGene; Hs.591405; -.
 PDB; 2OXC; X-ray; 1.30 A; A/B=41-268.
 PDB; 3B7G; X-ray; 1.90 A; A/B=41-268.
 PDBsum; 2OXC; -.
 PDBsum; 3B7G; -.
 ProteinModelPortal; Q9UHI6; -.
 SMR; Q9UHI6; -.
 BioGrid; 116387; 88.
 CORUM; Q9UHI6; -.
 DIP; DIP-32606N; -.
 IntAct; Q9UHI6; 49.
 MINT; Q9UHI6; -.
 STRING; 9606.ENSP00000358716; -.
 iPTMnet; Q9UHI6; -.
 PhosphoSitePlus; Q9UHI6; -.
 BioMuta; DDX20; -.
 DMDM; 12643886; -.
 EPD; Q9UHI6; -.
 PaxDb; Q9UHI6; -.
 PeptideAtlas; Q9UHI6; -.
 PRIDE; Q9UHI6; -.
 DNASU; 11218; -.
 Ensembl; ENST00000369702; ENSP00000358716; ENSG00000064703. [Q9UHI6-1]
 Ensembl; ENST00000533164; ENSP00000434085; ENSG00000064703. [Q9UHI6-2]
 GeneID; 11218; -.
 KEGG; hsa:11218; -.
 UCSC; uc001ebs.4; human. [Q9UHI6-1]
 CTD; 11218; -.
 DisGeNET; 11218; -.
 EuPathDB; HostDB:ENSG00000064703.11; -.
 GeneCards; DDX20; -.
 HGNC; HGNC:2743; DDX20.
 HPA; CAB015427; -.
 HPA; HPA005516; -.
 HPA; HPA023541; -.
 MIM; 606168; gene.
 neXtProt; NX_Q9UHI6; -.
 OpenTargets; ENSG00000064703; -.
 PharmGKB; PA27209; -.
 eggNOG; KOG4284; Eukaryota.
 eggNOG; COG0513; LUCA.
 GeneTree; ENSGT00910000144284; -.
 HOGENOM; HOG000112184; -.
 HOVERGEN; HBG051330; -.
 InParanoid; Q9UHI6; -.
 KO; K13131; -.
 OMA; QDYEEYW; -.
 OrthoDB; EOG091G0461; -.
 PhylomeDB; Q9UHI6; -.
 TreeFam; TF352222; -.
 Reactome; R-HSA-191859; snRNP Assembly.
 SIGNOR; Q9UHI6; -.
 EvolutionaryTrace; Q9UHI6; -.
 GeneWiki; DDX20; -.
 GenomeRNAi; 11218; -.
 PRO; PR:Q9UHI6; -.
 Proteomes; UP000005640; Chromosome 1.
 Bgee; ENSG00000064703; -.
 CleanEx; HS_DDX20; -.
 ExpressionAtlas; Q9UHI6; baseline and differential.
 Genevisible; Q9UHI6; HS.
 GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
 GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
 GO; GO:0005829; C:cytosol; IDA:UniProtKB.
 GO; GO:0097504; C:Gemini of coiled bodies; IEA:UniProtKB-SubCell.
 GO; GO:0016020; C:membrane; HDA:UniProtKB.
 GO; GO:0005730; C:nucleolus; IBA:GO_Central.
 GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO; GO:0005634; C:nucleus; TAS:ProtInc.
 GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IEA:Ensembl.
 GO; GO:0032797; C:SMN complex; IDA:UniProtKB.
 GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO; GO:0004004; F:ATP-dependent RNA helicase activity; TAS:ProtInc.
 GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
 GO; GO:0030674; F:protein binding, bridging; IEA:Ensembl.
 GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
 GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL.
 GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
 GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
 GO; GO:0051170; P:nuclear import; TAS:Reactome.
 GO; GO:0048477; P:oogenesis; IEA:Ensembl.
 GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
 GO; GO:0050810; P:regulation of steroid biosynthetic process; IEA:Ensembl.
 GO; GO:0006396; P:RNA processing; TAS:ProtInc.
 GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central.
 GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
 GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; TAS:ProtInc.
 CDD; cd00079; HELICc; 1.
 InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
 InterPro; IPR014001; Helicase_ATP-bd.
 InterPro; IPR001650; Helicase_C.
 InterPro; IPR027417; P-loop_NTPase.
 InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
 InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
 Pfam; PF00270; DEAD; 1.
 Pfam; PF00271; Helicase_C; 1.
 SMART; SM00487; DEXDc; 1.
 SMART; SM00490; HELICc; 1.
 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; Alternative splicing; ATP-binding; Complete proteome;
 Cytoplasm; DNA-binding; Helicase; Hydrolase; mRNA processing;
 mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
 Polymorphism; Reference proteome.
 CHAIN         1    824       Probable ATP-dependent RNA helicase
                              DDX20.
                              /FTId=PRO_0000055025.
 DOMAIN       93    264       Helicase ATP-binding.
                              {ECO:0000255|PROSITE-ProRule:PRU00541}.
 DOMAIN      299    448       Helicase C-terminal.
                              {ECO:0000255|PROSITE-ProRule:PRU00542}.
 NP_BIND     109    114       ATP.
 REGION      456    548       SMN interacting.
 MOTIF        62     90       Q motif.
 MOTIF       211    214       DEAD box.
 BINDING      84     84       ATP; via carbonyl oxygen.
 BINDING      89     89       ATP.
 MOD_RES      48     48       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     187    187       Phosphoserine.
                              {ECO:0000244|PubMed:18691976}.
 MOD_RES     268    268       Phosphoserine.
                              {ECO:0000244|PubMed:23186163}.
 MOD_RES     269    269       Phosphoserine.
                              {ECO:0000244|PubMed:23186163}.
 MOD_RES     500    500       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     505    505       Phosphoserine.
                              {ECO:0000244|PubMed:21406692,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     532    532       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     552    552       Phosphothreonine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:18691976,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     560    560       Phosphoserine.
                              {ECO:0000244|PubMed:23186163}.
 MOD_RES     652    652       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     654    654       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     656    656       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     672    672       Phosphoserine.
                              {ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:21406692,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     677    677       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:21406692,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     678    678       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:21406692,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     688    688       Phosphothreonine.
                              {ECO:0000244|PubMed:16964243}.
 MOD_RES     703    703       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     705    705       Phosphothreonine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     714    714       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:18691976,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:23186163}.
 VAR_SEQ     133    138       ILILAP -> AELSNS (in isoform 2).
                              {ECO:0000303|PubMed:14702039}.
                              /FTId=VSP_056505.
 VAR_SEQ     139    824       Missing (in isoform 2).
                              {ECO:0000303|PubMed:14702039}.
                              /FTId=VSP_056506.
 VARIANT     636    636       I -> T (in dbSNP:rs197412).
                              {ECO:0000269|PubMed:15489334}.
                              /FTId=VAR_057231.
 VARIANT     693    693       R -> S (in dbSNP:rs197414).
                              /FTId=VAR_057232.
 VARIANT     762    762       I -> T (in dbSNP:rs85276).
                              /FTId=VAR_057233.
 CONFLICT      5      5       F -> V (in Ref. 2; AAD42744).
                              {ECO:0000305}.
 CONFLICT    279    279       Y -> C (in Ref. 3; BAA91727).
                              {ECO:0000305}.
 CONFLICT    639    639       R -> K (in Ref. 1; AAF14544).
                              {ECO:0000305}.
 CONFLICT    659    659       Y -> H (in Ref. 2; AAD42744).
                              {ECO:0000305}.
 CONFLICT    676    676       G -> S (in Ref. 1; AAF14544).
                              {ECO:0000305}.
 CONFLICT    703    703       S -> T (in Ref. 1; AAF14544).
                              {ECO:0000305}.
 HELIX        64     67       {ECO:0000244|PDB:2OXC}.
 HELIX        71     79       {ECO:0000244|PDB:2OXC}.
 HELIX        87     97       {ECO:0000244|PDB:2OXC}.
 STRAND      102    105       {ECO:0000244|PDB:2OXC}.
 HELIX       112    123       {ECO:0000244|PDB:2OXC}.
 STRAND      133    136       {ECO:0000244|PDB:2OXC}.
 HELIX       140    153       {ECO:0000244|PDB:2OXC}.
 TURN        154    156       {ECO:0000244|PDB:2OXC}.
 STRAND      162    165       {ECO:0000244|PDB:2OXC}.
 HELIX       171    177       {ECO:0000244|PDB:2OXC}.
 STRAND      182    186       {ECO:0000244|PDB:2OXC}.
 HELIX       188    196       {ECO:0000244|PDB:2OXC}.
 HELIX       202    204       {ECO:0000244|PDB:2OXC}.
 STRAND      207    212       {ECO:0000244|PDB:2OXC}.
 HELIX       213    217       {ECO:0000244|PDB:2OXC}.
 HELIX       223    232       {ECO:0000244|PDB:2OXC}.
 STRAND      238    244       {ECO:0000244|PDB:2OXC}.
 HELIX       248    254       {ECO:0000244|PDB:2OXC}.
 TURN        255    257       {ECO:0000244|PDB:2OXC}.
 STRAND      262    264       {ECO:0000244|PDB:2OXC}.
 SEQUENCE   824 AA;  92241 MW;  76712F014B2A0CF2 CRC64;
 MAAAFEASGA LAAVATAMPA EHVAVQVPAP EPTPGPVRIL RTAQDLSSPR TRTGDVLLAE
 PADFESLLLS RPVLEGLRAA GFERPSPVQL KAIPLGRCGL DLIVQAKSGT GKTCVFSTIA
 LDSLVLENLS TQILILAPTR EIAVQIHSVI TAIGIKMEGL ECHVFIGGTP LSQDKTRLKK
 CHIAVGSPGR IKQLIELDYL NPGSIRLFIL DEADKLLEEG SFQEQINWIY SSLPASKQML
 AVSATYPEFL ANALTKYMRD PTFVRLNSSD PSLIGLKQYY KVVNSYPLAH KVFEEKTQHL
 QELFSRIPFN QALVFSNLHS RAQHLADILS SKGFPAECIS GNMNQNQRLD AMAKLKHFHC
 RVLISTDLTS RGIDAEKVNL VVNLDVPLDW ETYMHRIGRA GRFGTLGLTV TYCCRGEEEN
 MMMRIAQKCN INLLPLPDPI PSGLMEECVD WDVEVKAAVH TYGIASVPNQ PLKKQIQKIE
 RTLQIQKAHG DHMASSRNNS VSGLSVKSKN NTKQKLPVKS HSECGIIEKA TSPKELGCDR
 QSEEQMKNSV QTPVENSTNS QHQVKEALPV SLPQIPCLSS FKIHQPYTLT FAELVEDYEH
 YIKEGLEKPV EIIRHYTGPG DQTVNPQNGF VRNKVIEQRV PVLASSSQSG DSESDSDSYS
 SRTSSQSKGN KSYLEGSSDN QLKDSESTPV DDRISLEQPP NGSDTPNPEK YQESPGIQMK
 TRLKEGASQR AKQSRRNLPR RSSFRLQTEA QEDDWYDCHR EIRLSFSDTY QDYEEYWRAY
 YRAWQEYYAA ASHSYYWNAQ RHPSWMAAYH MNTIYLQEMM HSNQ

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