ID DDX56_HUMAN Reviewed; 547 AA. AC Q9NY93; A4D2K9; C9JV95; Q6IAE2; Q9H9I8; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 202. DE RecName: Full=Probable ATP-dependent RNA helicase DDX56; DE EC=3.6.4.13; DE AltName: Full=ATP-dependent 61 kDa nucleolar RNA helicase; DE AltName: Full=DEAD box protein 21; DE AltName: Full=DEAD box protein 56; GN Name=DDX56; Synonyms=DDX21, NOH61; 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). RC TISSUE=Keratinocyte; RX PubMed=10749921; DOI=10.1091/mbc.11.4.1153; RA Zirwes R.F., Eilbracht J., Kneissel S., Schmidt-Zachmann M.S.; RT "A novel helicase-type protein in the nucleolus: protein NOH61."; RL Mol. Biol. Cell 11:1153-1167(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Camargo A.A., Nunes D.N., Samaia H.B., Simpson A.J.G., Dias-Neto E.; RT "Sequencing of a new human DEAD-box RNA helicase."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Fetal brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Glial tumor; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271; RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., RA Greco A., Hochstrasser D.F., Diaz J.-J.; RT "Functional proteomic analysis of human nucleolus."; RL Mol. Biol. Cell 13:4100-4109(2002). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [12] 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 [13] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH WEST NILE VIRUS CAPSID RP PROTEIN C (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP ASP-166 AND GLU-167. RX PubMed=22925334; DOI=10.1016/j.virol.2012.08.011; RA Xu Z., Hobman T.C.; RT "The helicase activity of DDX56 is required for its role in assembly of RT infectious West Nile virus particles."; RL Virology 433:226-235(2012). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141 AND SER-532, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP FUNCTION, INTERACTION WITH IRF3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP ASP-166 AND GLU-167. RX PubMed=31340999; DOI=10.1242/jcs.230409; RA Li D., Fu S., Wu Z., Yang W., Ru Y., Shu H., Liu X., Zheng H.; RT "DDX56 inhibits type I interferon by disrupting assembly of IRF3-IPO5 to RT inhibit IRF3 nucleus import."; RL J. Cell Sci. 133:0-0(2019). RN [17] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH FOOT-AND-MOUTH DISEASE RP VIRUS PROTEIN 3A (MICROBIAL INFECTION). RX PubMed=31445188; DOI=10.1016/j.cellsig.2019.109393; RA Fu S.Z., Yang W.P., Ru Y., Zhang K.S., Wang Y., Liu X.T., Li D., RA Zheng H.X.; RT "DDX56 cooperates with FMDV 3A to enhance FMDV replication by inhibiting RT the phosphorylation of IRF3."; RL Cell. Signal. 64:109393-109393(2019). RN [18] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=33789112; DOI=10.1016/j.celrep.2021.108903; RA Pryszlak M., Wiggans M., Chen X., Jaramillo J.E., Burns S.E., RA Richards L.M., Pugh T.J., Kaplan D.R., Huang X., Dirks P.B., Pearson B.J.; RT "The DEAD-box helicase DDX56 is a conserved stemness regulator in normal RT and cancer stem cells."; RL Cell Rep. 34:108903-108903(2021). RN [19] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=34922148; DOI=10.1016/j.vetmic.2021.109304; RA Xu S., Xie J., Zhang X., Chen L., Bi Y., Li X., Idris A., Feng R.; RT "DDX56 antagonizes IFN-beta production to enhance EMCV replication by RT inhibiting IRF3 nuclear translocation."; RL Vet. Microbiol. 264:109304-109304(2022). CC -!- FUNCTION: Nucleolar RNA helicase that plays a role in various CC biological processes including innate immunity, ribosome biogenesis or CC nucleolus organization (PubMed:31340999, PubMed:33789112). Plays an CC essential role in maintaining nucleolar integrity in planarian stem CC cells (PubMed:33789112). Maintains embryonic stem cells proliferation CC by conventional regulation of ribosome assembly and interaction with CC OCT4 and POU5F1 complex (By similarity). Regulates antiviral innate CC immunity by inhibiting the virus-triggered signaling nuclear CC translocation of IRF3 (PubMed:31340999). Mechanistically, acts by CC disrupting the interaction between IRF3 and importin IPO5 CC (PubMed:31340999). May play a role in later stages of the processing of CC the pre-ribosomal particles leading to mature 60S ribosomal subunits. CC Has intrinsic ATPase activity. {ECO:0000250|UniProtKB:Q9D0R4, CC ECO:0000269|PubMed:31340999, ECO:0000269|PubMed:33789112}. CC -!- FUNCTION: (Microbial infection) Helicase activity is important for CC packaging viral RNA into virions during West Nile virus infection. CC {ECO:0000269|PubMed:22925334}. CC -!- FUNCTION: (Microbial infection) Plays a positive role in foot-and-mouth CC disease virus replication by inhibiting the phosphorylation of IRF3 CC leading to inhibition of type I interferon. CC {ECO:0000269|PubMed:31445188}. CC -!- FUNCTION: (Microbial infection) Plays a positive role in EMCV CC replication by interrupting IRF3 phosphorylation and its nucleus CC translocation. {ECO:0000269|PubMed:34922148}. 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: May form homooligomeric complexes. Interacts with IRF3 CC (PubMed:31340999). Interacts with OCT4 and POU5F1 (By similarity). CC {ECO:0000250|UniProtKB:Q9D0R4, ECO:0000269|PubMed:31340999}. CC -!- SUBUNIT: (Microbial infection) Interacts with West Nile virus capsid CC protein C. {ECO:0000269|PubMed:22925334}. CC -!- SUBUNIT: (Microbial infection) Interacts with foot-and-mouth disease CC virus protein 3A; this interaction leads to inhibition of type I CC interferon production. {ECO:0000269|PubMed:31445188}. CC -!- SUBUNIT: (Microbial infection) Interacts with EMCV protein 3C; this CC interaction leads to inhibition of type I interferon production. CC {ECO:0000269|PubMed:31445188}. CC -!- INTERACTION: CC Q9NY93; P38919: EIF4A3; NbExp=3; IntAct=EBI-372376, EBI-299104; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, CC ECO:0000269|PubMed:22925334, ECO:0000269|PubMed:31340999, CC ECO:0000269|PubMed:33789112}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NY93-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NY93-2; Sequence=VSP_044869; CC -!- TISSUE SPECIFICITY: Detected in heart, brain, liver, pancreas, placenta CC and lung. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX56/DBP9 CC subfamily. {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; AJ131712; CAB87992.1; -; mRNA. DR EMBL; AF247666; AAG36876.1; -; mRNA. DR EMBL; AL136700; CAB66635.1; -; mRNA. DR EMBL; AK022774; BAB14238.1; -; mRNA. DR EMBL; AK315363; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CR457213; CAG33494.1; -; mRNA. DR EMBL; AC004938; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH236960; EAL23752.1; -; Genomic_DNA. DR EMBL; CH471128; EAW61094.1; -; Genomic_DNA. DR EMBL; BC001235; AAH01235.1; -; mRNA. DR CCDS; CCDS5492.1; -. [Q9NY93-1] DR CCDS; CCDS59053.1; -. [Q9NY93-2] DR RefSeq; NP_001244118.1; NM_001257189.1. [Q9NY93-2] DR RefSeq; NP_061955.1; NM_019082.3. [Q9NY93-1] DR AlphaFoldDB; Q9NY93; -. DR SMR; Q9NY93; -. DR BioGRID; 120075; 328. DR IntAct; Q9NY93; 90. DR MINT; Q9NY93; -. DR STRING; 9606.ENSP00000258772; -. DR iPTMnet; Q9NY93; -. DR MetOSite; Q9NY93; -. DR PhosphoSitePlus; Q9NY93; -. DR SwissPalm; Q9NY93; -. DR BioMuta; DDX56; -. DR DMDM; 20139238; -. DR EPD; Q9NY93; -. DR jPOST; Q9NY93; -. DR MassIVE; Q9NY93; -. DR MaxQB; Q9NY93; -. DR PaxDb; 9606-ENSP00000258772; -. DR PeptideAtlas; Q9NY93; -. DR ProteomicsDB; 11840; -. DR ProteomicsDB; 83197; -. [Q9NY93-1] DR Pumba; Q9NY93; -. DR Antibodypedia; 13419; 409 antibodies from 27 providers. DR DNASU; 54606; -. DR Ensembl; ENST00000258772.10; ENSP00000258772.5; ENSG00000136271.11. [Q9NY93-1] DR Ensembl; ENST00000431640.5; ENSP00000393488.1; ENSG00000136271.11. [Q9NY93-2] DR GeneID; 54606; -. DR KEGG; hsa:54606; -. DR MANE-Select; ENST00000258772.10; ENSP00000258772.5; NM_019082.4; NP_061955.1. DR UCSC; uc003tlg.5; human. [Q9NY93-1] DR AGR; HGNC:18193; -. DR CTD; 54606; -. DR DisGeNET; 54606; -. DR GeneCards; DDX56; -. DR HGNC; HGNC:18193; DDX56. DR HPA; ENSG00000136271; Low tissue specificity. DR MIM; 608023; gene. DR neXtProt; NX_Q9NY93; -. DR OpenTargets; ENSG00000136271; -. DR PharmGKB; PA134916346; -. DR VEuPathDB; HostDB:ENSG00000136271; -. DR eggNOG; KOG0346; Eukaryota. DR GeneTree; ENSGT00550000074946; -. DR HOGENOM; CLU_003041_17_1_1; -. DR InParanoid; Q9NY93; -. DR OMA; GDIDRCY; -. DR OrthoDB; 227126at2759; -. DR PhylomeDB; Q9NY93; -. DR TreeFam; TF300620; -. DR PathwayCommons; Q9NY93; -. DR SignaLink; Q9NY93; -. DR BioGRID-ORCS; 54606; 848 hits in 1169 CRISPR screens. DR ChiTaRS; DDX56; human. DR GeneWiki; DDX56; -. DR GenomeRNAi; 54606; -. DR Pharos; Q9NY93; Tbio. DR PRO; PR:Q9NY93; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9NY93; Protein. DR Bgee; ENSG00000136271; Expressed in lower esophagus mucosa and 197 other cell types or tissues. DR ExpressionAtlas; Q9NY93; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:FlyBase. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:LIFEdb. DR GO; GO:0005634; C:nucleus; IDA:UniProt. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0140311; F:protein sequestering activity; IDA:UniProt. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003724; F:RNA helicase activity; TAS:ProtInc. DR GO; GO:0035613; F:RNA stem-loop binding; IDA:FlyBase. DR GO; GO:0051607; P:defense response to virus; IDA:FlyBase. DR GO; GO:0044830; P:modulation by host of viral RNA genome replication; IMP:FlyBase. DR GO; GO:0032480; P:negative regulation of type I interferon production; IDA:UniProt. DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR CDD; cd17961; DEADc_DDX56; 1. DR CDD; cd18787; SF2_C_DEAD; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1. DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. DR SWISS-2DPAGE; Q9NY93; -. DR Genevisible; Q9NY93; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Helicase; Hydrolase; Nucleotide-binding; KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis; KW RNA-binding; rRNA processing. FT CHAIN 1..547 FT /note="Probable ATP-dependent RNA helicase DDX56" FT /id="PRO_0000055058" FT DOMAIN 38..218 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 230..424 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 506..547 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 7..35 FT /note="Q motif" FT MOTIF 166..169 FT /note="DEAD box" FT BINDING 51..58 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT MOD_RES 126 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 141 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 532 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 298..337 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044869" FT MUTAGEN 166 FT /note="D->N: Complete loss of interaction with IRF3. About FT 3-4 times less genomic RNA in West Nile virus particles." FT /evidence="ECO:0000269|PubMed:17525332, FT ECO:0000269|PubMed:22925334" FT MUTAGEN 167 FT /note="E->Q: Complete loss of interaction with IRF3. About FT 3-4 times less genomic RNA in West Nile virus particles." FT /evidence="ECO:0000269|PubMed:17525332, FT ECO:0000269|PubMed:22925334" FT CONFLICT 30 FT /note="P -> S (in Ref. 5; CAG33494)" FT /evidence="ECO:0000305" FT CONFLICT 145 FT /note="I -> T (in Ref. 4; BAB14238)" FT /evidence="ECO:0000305" FT CONFLICT 402 FT /note="E -> D (in Ref. 4; AK315363)" FT /evidence="ECO:0000305" FT CONFLICT 518 FT /note="C -> Y (in Ref. 5; CAG33494)" FT /evidence="ECO:0000305" SQ SEQUENCE 547 AA; 61590 MW; 6D127CDAA73610D2 CRC64; MEDSEALGFE HMGLDPRLLQ AVTDLGWSRP TLIQEKAIPL ALEGKDLLAR ARTGSGKTAA YAIPMLQLLL HRKATGPVVE QAVRGLVLVP TKELARQAQS MIQQLATYCA RDVRVANVSA AEDSVSQRAV LMEKPDVVVG TPSRILSHLQ QDSLKLRDSL ELLVVDEADL LFSFGFEEEL KSLLCHLPRI YQAFLMSATF NEDVQALKEL ILHNPVTLKL QESQLPGPDQ LQQFQVVCET EEDKFLLLYA LLKLSLIRGK SLLFVNTLER SYRLRLFLEQ FSIPTCVLNG ELPLRSRCHI ISQFNQGFYD CVIATDAEVL GAPVKGKRRG RGPKGDKASD PEAGVARGID FHHVSAVLNF DLPPTPEAYI HRAGRTARAN NPGIVLTFVL PTEQFHLGKI EELLSGENRG PILLPYQFRM EEIEGFRYRC RDAMRSVTKQ AIREARLKEI KEELLHSEKL KTYFEDNPRD LQLLRHDLPL HPAVVKPHLG HVPDYLVPPA LRGLVRPHKK RKKLSSSCRK AKRAKSQNPL RSFKHKGKKF RPTAKPS //