ID DDX20_HUMAN Reviewed; 824 AA. AC Q9UHI6; B4DWV7; Q96F72; Q9NVM3; Q9UF59; Q9UIY0; Q9Y659; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-DEC-2019, entry version 212. DE RecName: Full=Probable ATP-dependent RNA helicase DDX20; DE EC=3.6.4.13; DE AltName: Full=Component of gems 3; DE AltName: Full=DEAD box protein 20; DE AltName: Full=DEAD box protein DP 103; DE AltName: Full=Gemin-3; GN Name=DDX20; Synonyms=DP103, GEMIN3; 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), IDENTIFICATION IN THE CORE SMN RP COMPLEX, INTERACTION WITH SNRPB; SNRPD2 AND SNRPD3, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=10601333; DOI=10.1083/jcb.147.6.1181; RA Charroux B., Pellizzoni L., Perkinson R.A., Shevchenko A., Mann M., RA Dreyfuss G.; RT "Gemin3: a novel DEAD box protein that interacts with SMN, the spinal RT muscular atrophy gene product, and a component of gems."; RL J. Cell Biol. 147:1181-1194(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH EBV EBNA2 AND RP EBV EBNA3C. RX PubMed=10383418; DOI=10.1074/jbc.274.27.19136; RA Grundhoff A.T., Kremmer E., Tuereci O., Glieden A., Gindorf C., Atz J., RA Mueller-Lantzsch N., Schubach W.H., Grasser F.A.; RT "Characterization of DP103, a novel DEAD box protein that binds to the RT Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C."; RL J. Biol. Chem. 274:19136-19144(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Esophagus; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-636. RC TISSUE=Placenta; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-275 (ISOFORM 1). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP INTERACTION WITH SNUPN; SMN1 AND SNRPB. RX PubMed=12095920; DOI=10.1093/hmg/11.15.1785; RA Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.; RT "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex RT with snurportin1 and importin beta."; RL Hum. Mol. Genet. 11:1785-1795(2002). RN [8] RP INTERACTION WITH PPP4R2. RX PubMed=12668731; DOI=10.1242/jcs.00409; RA Carnegie G.K., Sleeman J.E., Morrice N., Hastie C.J., Peggie M.W., RA Philp A., Lamond A.I., Cohen P.T.W.; RT "Protein phosphatase 4 interacts with the survival of motor neurons complex RT and enhances the temporal localisation of snRNPs."; RL J. Cell Sci. 116:1905-1913(2003). RN [9] RP INTERACTION WITH FOXL2. RX PubMed=16153597; DOI=10.1016/j.bbrc.2005.08.184; RA Lee K., Pisarska M.D., Ko J.J., Kang Y., Yoon S., Ryou S.M., Cha K.Y., RA Bae J.; RT "Transcriptional factor FOXL2 interacts with DP103 and induces apoptosis."; RL Biochem. Biophys. Res. Commun. 336:876-881(2005). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-688, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [11] RP FUNCTION IN SNRNP BIOGENESIS, AND IDENTIFICATION IN SMN-SM COMPLEX. RX PubMed=18984161; DOI=10.1016/j.cell.2008.09.020; RA Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., RA Englbrecht C., Sickmann A., Stark H., Fischer U.; RT "An assembly chaperone collaborates with the SMN complex to generate RT spliceosomal SnRNPs."; RL Cell 135:497-509(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; THR-552 AND SER-714, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-500; SER-532; RP THR-552; SER-652; SER-654; SER-656; SER-677; SER-678; SER-703; THR-705 AND RP SER-714, AND 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 [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677; SER-678 AND SER-703, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672; SER-678 AND SER-714, AND RP IDENTIFICATION BY 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 [17] 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 [18] RP INTERACTION WITH PUM2 AND NANOS1. RX PubMed=21800163; DOI=10.1007/s00418-011-0842-y; RA Ginter-Matuszewska B., Kusz K., Spik A., Grzeszkowiak D., Rembiszewska A., RA Kupryjanczyk J., Jaruzelska J.; RT "NANOS1 and PUMILIO2 bind microRNA biogenesis factor GEMIN3, within RT chromatoid body in human germ cells."; RL Histochem. Cell Biol. 136:279-287(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505; SER-672; SER-677 AND RP SER-678, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268; SER-269; SER-505; RP THR-552; SER-560; SER-672; SER-677; SER-678; SER-703; THR-705 AND SER-714, RP AND 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 [21] RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 41-268 IN COMPLEX WITH ADP, AND RP ADP-BINDING. RX PubMed=20510246; DOI=10.1016/j.jmb.2010.05.046; RA Schutz P., Wahlberg E., Karlberg T., Hammarstrom M., Collins R., Flores A., RA Schuler H.; RT "Crystal structure of human RNA helicase A (DHX9): structural basis for RT unselective nucleotide base binding in a DEAD-box variant protein."; RL J. Mol. Biol. 400:768-782(2010). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 41-268. 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: The SMN complex plays a catalyst role in the assembly of CC small nuclear ribonucleoproteins (snRNPs), the building blocks of the CC spliceosome. Thereby, plays an important role in the splicing of CC cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm CC proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that CC assemble in a heptameric protein ring on the Sm site of the small CC nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins CC SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S CC pICln-Sm complex by the chaperone CLNS1A that controls the assembly of CC the core snRNP. Dissociation by the SMN complex of CLNS1A from the CC trapped Sm proteins and their transfer to an SMN-Sm complex triggers CC the assembly of core snRNPs and their transport to the nucleus. May CC also play a role in the metabolism of small nucleolar ribonucleoprotein CC (snoRNPs). {ECO:0000269|PubMed:18984161}. 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: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. CC Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and CC the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. CC Interacts directly with GEMIN5. Interacts directly with SNUPN. CC Interacts with PPP4R2. Interacts with FOXL2. Interacts with EBV EBNA2 CC and EBNA3C. Interacts with NANOS1 and PUM2. CC {ECO:0000269|PubMed:10383418, ECO:0000269|PubMed:10601333, CC ECO:0000269|PubMed:12095920, ECO:0000269|PubMed:12668731, CC ECO:0000269|PubMed:16153597, ECO:0000269|PubMed:18984161, CC ECO:0000269|PubMed:20510246, ECO:0000269|PubMed:21800163}. CC -!- INTERACTION: CC P57678:GEMIN4; NbExp=6; IntAct=EBI-347658, EBI-356700; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, gem. Note=Localized in CC subnuclear structures next to coiled bodies, called Gemini of Cajal CC bodies (Gems). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UHI6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UHI6-2; Sequence=VSP_056505, VSP_056506; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX20 subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF171063; AAF14544.1; -; mRNA. DR EMBL; AF106019; AAD42744.1; -; mRNA. DR EMBL; AK001506; BAA91727.1; -; mRNA. DR EMBL; AK301697; BAG63169.1; -; mRNA. DR EMBL; AL049557; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC011556; AAH11556.1; -; mRNA. DR EMBL; AL133598; CAB63734.2; -; mRNA. DR CCDS; CCDS842.1; -. [Q9UHI6-1] DR PIR; T43476; T43476. DR RefSeq; NP_009135.4; NM_007204.4. [Q9UHI6-1] DR PDB; 2OXC; X-ray; 1.30 A; A/B=41-268. DR PDB; 3B7G; X-ray; 1.90 A; A/B=41-268. DR PDBsum; 2OXC; -. DR PDBsum; 3B7G; -. DR SMR; Q9UHI6; -. DR BioGrid; 116387; 101. DR CORUM; Q9UHI6; -. DR DIP; DIP-32606N; -. DR IntAct; Q9UHI6; 54. DR MINT; Q9UHI6; -. DR STRING; 9606.ENSP00000358716; -. DR iPTMnet; Q9UHI6; -. DR PhosphoSitePlus; Q9UHI6; -. DR BioMuta; DDX20; -. DR DMDM; 12643886; -. DR EPD; Q9UHI6; -. DR jPOST; Q9UHI6; -. DR MassIVE; Q9UHI6; -. DR PaxDb; Q9UHI6; -. DR PeptideAtlas; Q9UHI6; -. DR PRIDE; Q9UHI6; -. DR ProteomicsDB; 5385; -. DR ProteomicsDB; 84357; -. [Q9UHI6-1] DR DNASU; 11218; -. DR Ensembl; ENST00000369702; ENSP00000358716; ENSG00000064703. [Q9UHI6-1] DR Ensembl; ENST00000533164; ENSP00000434085; ENSG00000064703. [Q9UHI6-2] DR GeneID; 11218; -. DR KEGG; hsa:11218; -. DR UCSC; uc001ebs.4; human. [Q9UHI6-1] DR CTD; 11218; -. DR DisGeNET; 11218; -. DR EuPathDB; HostDB:ENSG00000064703.11; -. DR GeneCards; DDX20; -. DR HGNC; HGNC:2743; DDX20. DR HPA; CAB015427; -. DR HPA; HPA005516; -. DR MIM; 606168; gene. DR neXtProt; NX_Q9UHI6; -. DR OpenTargets; ENSG00000064703; -. DR PharmGKB; PA27209; -. DR eggNOG; KOG4284; Eukaryota. DR eggNOG; COG0513; LUCA. DR GeneTree; ENSGT00940000158400; -. DR HOGENOM; HOG000112184; -. DR InParanoid; Q9UHI6; -. DR KO; K13131; -. DR OMA; AYHMNTV; -. DR OrthoDB; 453219at2759; -. DR PhylomeDB; Q9UHI6; -. DR TreeFam; TF352222; -. DR Reactome; R-HSA-191859; snRNP Assembly. DR SIGNOR; Q9UHI6; -. DR ChiTaRS; DDX20; human. DR EvolutionaryTrace; Q9UHI6; -. DR GeneWiki; DDX20; -. DR GenomeRNAi; 11218; -. DR Pharos; Q9UHI6; Tbio. DR PRO; PR:Q9UHI6; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9UHI6; protein. DR Bgee; ENSG00000064703; Expressed in 189 organ(s), highest expression level in testis. DR ExpressionAtlas; Q9UHI6; baseline and differential. DR Genevisible; Q9UHI6; HS. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0097504; C:Gemini of coiled bodies; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IEA:Ensembl. DR GO; GO:0032797; C:SMN complex; IDA:UniProtKB. DR GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl. DR GO; GO:0030674; F:protein binding, bridging; IEA:Ensembl. DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl. DR GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0003724; F:RNA helicase activity; TAS:ProtInc. DR GO; GO:0051170; P:import into nucleus; TAS:Reactome. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0048477; P:oogenesis; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI. DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IEA:Ensembl. DR GO; GO:0006396; P:RNA processing; TAS:ProtInc. DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB. DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; TAS:ProtInc. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; DNA-binding; KW Helicase; Hydrolase; mRNA processing; mRNA splicing; Nucleotide-binding; KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome. FT CHAIN 1..824 FT /note="Probable ATP-dependent RNA helicase DDX20" FT /id="PRO_0000055025" FT DOMAIN 93..264 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 299..448 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT NP_BIND 109..114 FT /note="ATP" FT REGION 456..548 FT /note="SMN interacting" FT MOTIF 62..90 FT /note="Q motif" FT MOTIF 211..214 FT /note="DEAD box" FT BINDING 84 FT /note="ATP; via carbonyl oxygen" FT BINDING 89 FT /note="ATP" FT MOD_RES 48 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648" FT MOD_RES 187 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18691976" FT MOD_RES 268 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 269 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 500 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648" FT MOD_RES 505 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163" FT MOD_RES 532 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648" FT MOD_RES 552 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:23186163" FT MOD_RES 560 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 652 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648" FT MOD_RES 654 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648" FT MOD_RES 656 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648" FT MOD_RES 672 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163" FT MOD_RES 677 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163" FT MOD_RES 678 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163" FT MOD_RES 688 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:16964243" FT MOD_RES 703 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:23186163" FT MOD_RES 705 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163" FT MOD_RES 714 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163" FT VAR_SEQ 133..138 FT /note="ILILAP -> AELSNS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056505" FT VAR_SEQ 139..824 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056506" FT VARIANT 636 FT /note="I -> T (in dbSNP:rs197412)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_057231" FT VARIANT 693 FT /note="R -> S (in dbSNP:rs197414)" FT /id="VAR_057232" FT VARIANT 762 FT /note="I -> T (in dbSNP:rs85276)" FT /id="VAR_057233" FT CONFLICT 5 FT /note="F -> V (in Ref. 2; AAD42744)" FT /evidence="ECO:0000305" FT CONFLICT 279 FT /note="Y -> C (in Ref. 3; BAA91727)" FT /evidence="ECO:0000305" FT CONFLICT 639 FT /note="R -> K (in Ref. 1; AAF14544)" FT /evidence="ECO:0000305" FT CONFLICT 659 FT /note="Y -> H (in Ref. 2; AAD42744)" FT /evidence="ECO:0000305" FT CONFLICT 676 FT /note="G -> S (in Ref. 1; AAF14544)" FT /evidence="ECO:0000305" FT CONFLICT 703 FT /note="S -> T (in Ref. 1; AAF14544)" FT /evidence="ECO:0000305" FT HELIX 64..67 FT /evidence="ECO:0000244|PDB:2OXC" FT HELIX 71..79 FT /evidence="ECO:0000244|PDB:2OXC" FT HELIX 87..97 FT /evidence="ECO:0000244|PDB:2OXC" FT STRAND 102..105 FT /evidence="ECO:0000244|PDB:2OXC" FT HELIX 112..123 FT /evidence="ECO:0000244|PDB:2OXC" FT STRAND 133..136 FT /evidence="ECO:0000244|PDB:2OXC" FT HELIX 140..153 FT /evidence="ECO:0000244|PDB:2OXC" FT TURN 154..156 FT /evidence="ECO:0000244|PDB:2OXC" FT STRAND 162..165 FT /evidence="ECO:0000244|PDB:2OXC" FT HELIX 171..177 FT /evidence="ECO:0000244|PDB:2OXC" FT STRAND 182..186 FT /evidence="ECO:0000244|PDB:2OXC" FT HELIX 188..196 FT /evidence="ECO:0000244|PDB:2OXC" FT HELIX 202..204 FT /evidence="ECO:0000244|PDB:2OXC" FT STRAND 207..212 FT /evidence="ECO:0000244|PDB:2OXC" FT HELIX 213..217 FT /evidence="ECO:0000244|PDB:2OXC" FT HELIX 223..232 FT /evidence="ECO:0000244|PDB:2OXC" FT STRAND 238..244 FT /evidence="ECO:0000244|PDB:2OXC" FT HELIX 248..254 FT /evidence="ECO:0000244|PDB:2OXC" FT TURN 255..257 FT /evidence="ECO:0000244|PDB:2OXC" FT STRAND 262..264 FT /evidence="ECO:0000244|PDB:2OXC" SQ 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 //