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 10-MAY-2017, entry version 188.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RP BY 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
RP AND EBV EBNA3C.
RX PubMed=10383418; DOI=10.1074/jbc.274.27.19136;
RA Grundhoff A.T., Kremmer E., Tuereci O., Glieden A., Gindorf C.,
RA Atz J., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RP 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
RT project: 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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
RT complex 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
RT complex 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
RT apoptosis.";
RL Biochem. Biophys. Res. Commun. 336:876-881(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-688, AND IDENTIFICATION
RP BY 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
RT phosphorylation 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
RP SER-714, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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
RT the 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
RP AND SER-714, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677; SER-678 AND
RP SER-703, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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
RP SER-714, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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.,
RA Rembiszewska A., 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
RP AND SER-678, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome 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
RP SER-714, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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,
RP AND ADP-BINDING.
RX PubMed=20510246; DOI=10.1016/j.jmb.2010.05.046;
RA Schutz P., Wahlberg E., Karlberg T., Hammarstrom M., Collins R.,
RA Flores A., Schuler H.;
RT "Crystal structure of human RNA helicase A (DHX9): structural basis
RT for unselective nucleotide base binding in a DEAD-box variant
RT 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.,
RA Hogbom M., Holmberg-Schiavone L., Tempel W., Park H.W.,
RA Hammarstrom M., Moche M., 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
CC the spliceosome. Thereby, plays an important role in the splicing
CC of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common
CC set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and
CC SNRPG that assemble in a heptameric protein ring on the Sm site of
CC the small nuclear RNA to form the core snRNP. In the cytosol, the
CC Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in
CC an inactive 6S pICln-Sm complex by the chaperone CLNS1A that
CC controls the assembly of the core snRNP. Dissociation by the SMN
CC complex of CLNS1A from the trapped Sm proteins and their transfer
CC to an SMN-Sm complex triggers the assembly of core snRNPs and
CC their transport to the nucleus. May also play a role in the
CC metabolism of small nucleolar ribonucleoprotein (snoRNPs).
CC {ECO:0000269|PubMed:18984161}.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1,
CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8
CC and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1,
CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8,
CC STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3,
CC SNRPE, SNRPF and SNRPG. Interacts directly with GEMIN5. Interacts
CC directly with SNUPN. Interacts with PPP4R2. Interacts with FOXL2.
CC Interacts with EBV EBNA2 and EBNA3C. Interacts with NANOS1 and
CC PUM2. {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=5; IntAct=EBI-347658, EBI-356700;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, gem. Note=Localized in
CC subnuclear structures next to coiled bodies, called Gemini of
CC Cajal 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 Note=No experimental confirmation available.;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX20
CC subfamily. {ECO:0000305}.
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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 UniGene; Hs.591405; -.
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 ProteinModelPortal; Q9UHI6; -.
DR SMR; Q9UHI6; -.
DR BioGrid; 116387; 76.
DR DIP; DIP-32606N; -.
DR IntAct; Q9UHI6; 27.
DR MINT; MINT-96973; -.
DR STRING; 9606.ENSP00000358716; -.
DR iPTMnet; Q9UHI6; -.
DR PhosphoSitePlus; Q9UHI6; -.
DR BioMuta; DDX20; -.
DR DMDM; 12643886; -.
DR EPD; Q9UHI6; -.
DR PaxDb; Q9UHI6; -.
DR PeptideAtlas; Q9UHI6; -.
DR PRIDE; Q9UHI6; -.
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 GeneCards; DDX20; -.
DR HGNC; HGNC:2743; DDX20.
DR HPA; CAB015427; -.
DR HPA; HPA005516; -.
DR HPA; HPA023541; -.
DR MIM; 606168; gene.
DR neXtProt; NX_Q9UHI6; -.
DR OpenTargets; ENSG00000064703; -.
DR PharmGKB; PA27209; -.
DR eggNOG; KOG4284; Eukaryota.
DR eggNOG; COG0513; LUCA.
DR GeneTree; ENSGT00530000062880; -.
DR HOGENOM; HOG000112184; -.
DR HOVERGEN; HBG051330; -.
DR InParanoid; Q9UHI6; -.
DR KO; K13131; -.
DR OMA; KSHSECG; -.
DR OrthoDB; EOG091G0461; -.
DR PhylomeDB; Q9UHI6; -.
DR TreeFam; TF352222; -.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR SIGNOR; Q9UHI6; -.
DR EvolutionaryTrace; Q9UHI6; -.
DR GeneWiki; DDX20; -.
DR GenomeRNAi; 11218; -.
DR PRO; PR:Q9UHI6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR Bgee; ENSG00000064703; -.
DR CleanEx; HS_DDX20; -.
DR ExpressionAtlas; Q9UHI6; baseline and differential.
DR Genevisible; Q9UHI6; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
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; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
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:0004004; F:ATP-dependent RNA helicase activity; TAS:ProtInc.
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:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
DR GO; GO:0051170; P:nuclear import; TAS:Reactome.
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:0010501; P:RNA secondary structure unwinding; IBA:GO_Central.
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; Complete proteome;
KW Cytoplasm; DNA-binding; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 824 Probable ATP-dependent RNA helicase
FT DDX20.
FT /FTId=PRO_0000055025.
FT DOMAIN 93 264 Helicase ATP-binding.
FT {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT DOMAIN 299 448 Helicase C-terminal.
FT {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT NP_BIND 109 114 ATP.
FT REGION 456 548 SMN interacting.
FT MOTIF 62 90 Q motif.
FT MOTIF 211 214 DEAD box.
FT BINDING 84 84 ATP; via carbonyl oxygen.
FT BINDING 89 89 ATP.
FT MOD_RES 48 48 Phosphoserine.
FT {ECO:0000244|PubMed:18669648}.
FT MOD_RES 187 187 Phosphoserine.
FT {ECO:0000244|PubMed:18691976}.
FT MOD_RES 268 268 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 269 269 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 500 500 Phosphoserine.
FT {ECO:0000244|PubMed:18669648}.
FT MOD_RES 505 505 Phosphoserine.
FT {ECO:0000244|PubMed:21406692,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 532 532 Phosphoserine.
FT {ECO:0000244|PubMed:18669648}.
FT MOD_RES 552 552 Phosphothreonine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:18691976,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 560 560 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 652 652 Phosphoserine.
FT {ECO:0000244|PubMed:18669648}.
FT MOD_RES 654 654 Phosphoserine.
FT {ECO:0000244|PubMed:18669648}.
FT MOD_RES 656 656 Phosphoserine.
FT {ECO:0000244|PubMed:18669648}.
FT MOD_RES 672 672 Phosphoserine.
FT {ECO:0000244|PubMed:20068231,
FT ECO:0000244|PubMed:21406692,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 677 677 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:19690332,
FT ECO:0000244|PubMed:21406692,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 678 678 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:19690332,
FT ECO:0000244|PubMed:20068231,
FT ECO:0000244|PubMed:21406692,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 688 688 Phosphothreonine.
FT {ECO:0000244|PubMed:16964243}.
FT MOD_RES 703 703 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:19690332,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 705 705 Phosphothreonine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 714 714 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:18691976,
FT ECO:0000244|PubMed:20068231,
FT ECO:0000244|PubMed:23186163}.
FT VAR_SEQ 133 138 ILILAP -> AELSNS (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_056505.
FT VAR_SEQ 139 824 Missing (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_056506.
FT VARIANT 636 636 I -> T (in dbSNP:rs197412).
FT {ECO:0000269|PubMed:15489334}.
FT /FTId=VAR_057231.
FT VARIANT 693 693 R -> S (in dbSNP:rs197414).
FT /FTId=VAR_057232.
FT VARIANT 762 762 I -> T (in dbSNP:rs85276).
FT /FTId=VAR_057233.
FT CONFLICT 5 5 F -> V (in Ref. 2; AAD42744).
FT {ECO:0000305}.
FT CONFLICT 279 279 Y -> C (in Ref. 3; BAA91727).
FT {ECO:0000305}.
FT CONFLICT 639 639 R -> K (in Ref. 1; AAF14544).
FT {ECO:0000305}.
FT CONFLICT 659 659 Y -> H (in Ref. 2; AAD42744).
FT {ECO:0000305}.
FT CONFLICT 676 676 G -> S (in Ref. 1; AAF14544).
FT {ECO:0000305}.
FT CONFLICT 703 703 S -> T (in Ref. 1; AAF14544).
FT {ECO:0000305}.
FT HELIX 64 67 {ECO:0000244|PDB:2OXC}.
FT HELIX 71 79 {ECO:0000244|PDB:2OXC}.
FT HELIX 87 97 {ECO:0000244|PDB:2OXC}.
FT STRAND 102 105 {ECO:0000244|PDB:2OXC}.
FT HELIX 112 123 {ECO:0000244|PDB:2OXC}.
FT STRAND 133 136 {ECO:0000244|PDB:2OXC}.
FT HELIX 140 153 {ECO:0000244|PDB:2OXC}.
FT TURN 154 156 {ECO:0000244|PDB:2OXC}.
FT STRAND 162 165 {ECO:0000244|PDB:2OXC}.
FT HELIX 171 177 {ECO:0000244|PDB:2OXC}.
FT STRAND 182 186 {ECO:0000244|PDB:2OXC}.
FT HELIX 188 196 {ECO:0000244|PDB:2OXC}.
FT HELIX 202 204 {ECO:0000244|PDB:2OXC}.
FT STRAND 207 212 {ECO:0000244|PDB:2OXC}.
FT HELIX 213 217 {ECO:0000244|PDB:2OXC}.
FT HELIX 223 232 {ECO:0000244|PDB:2OXC}.
FT STRAND 238 244 {ECO:0000244|PDB:2OXC}.
FT HELIX 248 254 {ECO:0000244|PDB:2OXC}.
FT TURN 255 257 {ECO:0000244|PDB:2OXC}.
FT STRAND 262 264 {ECO:0000244|PDB:2OXC}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 93 264 iprf:HELICASE_ATP_BIND_1 [T]
FT MYHIT 209 217 ipat:DEAD_ATP_HELICASE [T]
FT MYHIT 323 404 ismart:HELICc [T]
FT MYHIT 295 404 ipfam:Helicase_C [T]
FT MYHIT 87 248 ipfam:DEAD [T]
FT MYHIT 299 448 iprf:HELICASE_CTER [T]
FT MYHIT 81 279 ismart:DEXDc [T]
FT MYHIT 62 90 iprf:Q_MOTIF [T]
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
//
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