ID DD19B_HUMAN Reviewed; 479 AA. AC Q9UMR2; B3KNE9; B4DXS6; E7EMK4; Q6FIB7; Q6IAE0; Q96KE7; Q9H0U0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 207. DE RecName: Full=ATP-dependent RNA helicase DDX19B; DE EC=3.6.4.13 {ECO:0000269|PubMed:10428971}; DE AltName: Full=DEAD box RNA helicase DEAD5; DE AltName: Full=DEAD box protein 19B; GN Name=DDX19B; Synonyms=DBP5, DDX19, TDBP; 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), FUNCTION, CATALYTIC ACTIVITY, RP ASSOCIATION WITH NUCLEAR PORE COMPLEX, INTERACTION WITH NUP214, SUBCELLULAR RP LOCATION, AND MUTAGENESIS OF GLU-243. RX PubMed=10428971; DOI=10.1093/emboj/18.15.4332; RA Schmitt C., von Kobbe C., Bachi A., Pante N., Rodrigues J.P., Boscheron C., RA Rigaut G., Wilm M., Seraphin B., Carmo-Fonseca M., Izaurralde E.; RT "Dbp5, a DEAD-box protein required for mRNA export, is recruited to the RT cytoplasmic fibrils of nuclear pore complex via a conserved interaction RT with CAN/Nup159p."; RL EMBO J. 18:4332-4347(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Testis; RX PubMed=12219940; DOI=10.1071/rd01028; RA Yin L., Li J., Zhu H., Lin M., Cheng L., Wang Y., Zhou Z., Sha J.; RT "Identification and characterization of a gene coding a novel isoform of RT DEAD-box protein."; RL Reprod. Fertil. Dev. 14:185-189(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=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). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4). RC TISSUE=Mammary gland, Stomach, and Testis; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [7] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Ovary, and Skin; 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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 54-475 ALONE AND IN COMPLEX WITH RP RNA, AND REGULATION BY N-TERMINAL HELIX DOMAIN. RX PubMed=19244245; DOI=10.1074/jbc.c900018200; RA Collins R., Karlberg T., Lehtio L., Schutz P., van den Berg S., RA Dahlgren L.G., Hammarstrom M., Weigelt J., Schuler H.; RT "The DEXD/H-box RNA helicase DDX19 is regulated by an alpha-helical RT switch."; RL J. Biol. Chem. 284:10296-10300(2009). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 68-479 IN COMPLEX WITH NUP214 AND RP ATP ANALOG, ATP-BINDING SITES, AND MUTAGENESIS OF ASP-223; ILE-258; ARG-259 RP AND ARG-262. RX PubMed=19219046; DOI=10.1038/nsmb.1561; RA von Moeller H., Basquin C., Conti E.; RT "The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin RT NUP214 in a mutually exclusive manner."; RL Nat. Struct. Mol. Biol. 16:247-254(2009). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 1-300 IN COMPLEX WITH NUP214 AND RP ADP. RX PubMed=19208808; DOI=10.1073/pnas.0813267106; RA Napetschnig J., Kassube S.A., Debler E.W., Wong R.W., Blobel G., Hoelz A.; RT "Structural and functional analysis of the interaction between the RT nucleoporin Nup214 and the DEAD-box helicase Ddx19."; RL Proc. Natl. Acad. Sci. U.S.A. 106:3089-3094(2009). CC -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA export from the CC nucleus (PubMed:10428971). Rather than unwinding RNA duplexes, DDX19B CC functions as a remodeler of ribonucleoprotein particles, whereby CC proteins bound to nuclear mRNA are dissociated and replaced by CC cytoplasmic mRNA binding proteins (PubMed:10428971). CC {ECO:0000269|PubMed:10428971}. 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 Evidence={ECO:0000269|PubMed:10428971}; CC -!- SUBUNIT: Associates with the nuclear pore complex via interaction with CC NUP214 (PubMed:10428971, PubMed:19208808, PubMed:19219046). Interacts CC with NUP214 or RNA in a mutually exclusive manner (PubMed:19208808, CC PubMed:19219046, PubMed:19244245). {ECO:0000269|PubMed:10428971, CC ECO:0000269|PubMed:19208808, ECO:0000269|PubMed:19219046, CC ECO:0000269|PubMed:19244245}. CC -!- INTERACTION: CC Q9UMR2; P45973: CBX5; NbExp=3; IntAct=EBI-719232, EBI-78219; CC Q9UMR2; O43310-2: CTIF; NbExp=3; IntAct=EBI-719232, EBI-12180013; CC Q9UMR2; A9UHW6: MIF4GD; NbExp=11; IntAct=EBI-719232, EBI-373498; CC Q9UMR2; A9UHW6-2: MIF4GD; NbExp=6; IntAct=EBI-719232, EBI-9118295; CC Q9UMR2; P54274: TERF1; NbExp=2; IntAct=EBI-719232, EBI-710997; CC Q9UMR2; P37173: TGFBR2; NbExp=3; IntAct=EBI-719232, EBI-296151; CC Q9UMR2-1; P35658-1: NUP214; NbExp=9; IntAct=EBI-5773937, EBI-15757000; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10428971}. Nucleus, CC nucleoplasm {ECO:0000269|PubMed:10428971}. Note=Associates with the CC nuclear pore complex cytoplasmic fibrils. CC {ECO:0000269|PubMed:10428971}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9UMR2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UMR2-2; Sequence=VSP_015239; CC Name=3; CC IsoId=Q9UMR2-3; Sequence=VSP_041347; CC Name=4; CC IsoId=Q9UMR2-4; Sequence=VSP_044727, VSP_015239; CC -!- DOMAIN: The N-terminal extension helix acts as an autoinhibitory CC domain, preventing ATP hydrolysis, unless the N-terminus of the protein CC is displaced by RNA binding, allowing cleft closure to bring key side CC chains into position for catalysis. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5 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; AJ237946; CAB52189.1; -; mRNA. DR EMBL; AF353720; AAK40102.1; -; mRNA. DR EMBL; AL136639; CAB66574.1; -; mRNA. DR EMBL; CR457215; CAG33496.1; -; mRNA. DR EMBL; CR533509; CAG38540.1; -; mRNA. DR EMBL; AK027378; BAG51311.1; -; mRNA. DR EMBL; AK301938; BAG63358.1; -; mRNA. DR EMBL; AK302107; BAG63488.1; -; mRNA. DR EMBL; AK316346; BAH14717.1; -; mRNA. DR EMBL; AC012184; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471241; EAW51827.1; -; Genomic_DNA. DR EMBL; CH471241; EAW51831.1; -; Genomic_DNA. DR EMBL; CH471241; EAW51832.1; -; Genomic_DNA. DR EMBL; CH471241; EAW51834.1; -; Genomic_DNA. DR EMBL; BC003626; AAH03626.1; -; mRNA. DR EMBL; BC010008; AAH10008.1; -; mRNA. DR CCDS; CCDS10888.1; -. [Q9UMR2-1] DR CCDS; CCDS32475.1; -. [Q9UMR2-2] DR CCDS; CCDS42187.1; -. [Q9UMR2-3] DR CCDS; CCDS58478.1; -. [Q9UMR2-4] DR RefSeq; NP_001014449.1; NM_001014449.2. [Q9UMR2-3] DR RefSeq; NP_001014451.1; NM_001014451.2. [Q9UMR2-2] DR RefSeq; NP_001244101.1; NM_001257172.1. [Q9UMR2-4] DR RefSeq; NP_001244102.1; NM_001257173.1. [Q9UMR2-3] DR RefSeq; NP_001244103.1; NM_001257174.1. [Q9UMR2-3] DR RefSeq; NP_009173.1; NM_007242.5. [Q9UMR2-1] DR RefSeq; XP_006721190.1; XM_006721127.2. DR RefSeq; XP_016878379.1; XM_017022890.1. DR PDB; 3EWS; X-ray; 2.70 A; A/B=54-475. DR PDB; 3FHC; X-ray; 2.80 A; B=68-302. DR PDB; 3FHT; X-ray; 2.20 A; A/B=68-479. DR PDB; 3FMO; X-ray; 2.51 A; B=1-300. DR PDB; 3FMP; X-ray; 3.19 A; B/D=1-479. DR PDB; 3G0H; X-ray; 2.70 A; A=54-475. DR PDB; 6B4I; X-ray; 3.62 A; E/F=54-479. DR PDB; 6B4J; X-ray; 3.40 A; E/F=54-479. DR PDB; 6B4K; X-ray; 2.20 A; A/B=54-479. DR PDBsum; 3EWS; -. DR PDBsum; 3FHC; -. DR PDBsum; 3FHT; -. DR PDBsum; 3FMO; -. DR PDBsum; 3FMP; -. DR PDBsum; 3G0H; -. DR PDBsum; 6B4I; -. DR PDBsum; 6B4J; -. DR PDBsum; 6B4K; -. DR AlphaFoldDB; Q9UMR2; -. DR SMR; Q9UMR2; -. DR BioGRID; 116426; 314. DR DIP; DIP-48486N; -. DR IntAct; Q9UMR2; 103. DR MINT; Q9UMR2; -. DR STRING; 9606.ENSP00000399208; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyGen; Q9UMR2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UMR2; -. DR PhosphoSitePlus; Q9UMR2; -. DR BioMuta; DDX19B; -. DR DMDM; 10719979; -. DR EPD; Q9UMR2; -. DR jPOST; Q9UMR2; -. DR MassIVE; Q9UMR2; -. DR MaxQB; Q9UMR2; -. DR PaxDb; 9606-ENSP00000288071; -. DR PeptideAtlas; Q9UMR2; -. DR ProteomicsDB; 16960; -. DR ProteomicsDB; 85194; -. [Q9UMR2-1] DR ProteomicsDB; 85195; -. [Q9UMR2-2] DR ProteomicsDB; 85196; -. [Q9UMR2-3] DR Pumba; Q9UMR2; -. DR Antibodypedia; 16335; 361 antibodies from 36 providers. DR DNASU; 11269; -. DR Ensembl; ENST00000288071.11; ENSP00000288071.7; ENSG00000157349.17. [Q9UMR2-1] DR Ensembl; ENST00000355992.7; ENSP00000348271.3; ENSG00000157349.17. [Q9UMR2-2] DR Ensembl; ENST00000393657.6; ENSP00000377267.2; ENSG00000157349.17. [Q9UMR2-3] DR Ensembl; ENST00000451014.7; ENSP00000392639.3; ENSG00000157349.17. [Q9UMR2-4] DR Ensembl; ENST00000563392.5; ENSP00000456574.1; ENSG00000157349.17. [Q9UMR2-3] DR Ensembl; ENST00000568625.5; ENSP00000456757.1; ENSG00000157349.17. [Q9UMR2-3] DR GeneID; 11269; -. DR KEGG; hsa:11269; -. DR MANE-Select; ENST00000288071.11; ENSP00000288071.7; NM_007242.7; NP_009173.1. DR UCSC; uc002eyo.5; human. [Q9UMR2-1] DR AGR; HGNC:2742; -. DR CTD; 11269; -. DR DisGeNET; 11269; -. DR GeneCards; DDX19B; -. DR HGNC; HGNC:2742; DDX19B. DR HPA; ENSG00000157349; Low tissue specificity. DR MIM; 605812; gene. DR neXtProt; NX_Q9UMR2; -. DR OpenTargets; ENSG00000157349; -. DR PharmGKB; PA27208; -. DR VEuPathDB; HostDB:ENSG00000157349; -. DR eggNOG; KOG0332; Eukaryota. DR GeneTree; ENSGT00940000154417; -. DR HOGENOM; CLU_003041_1_0_1; -. DR InParanoid; Q9UMR2; -. DR OMA; DPQTYLH; -. DR OrthoDB; 1087080at2759; -. DR PhylomeDB; Q9UMR2; -. DR TreeFam; TF314957; -. DR BRENDA; 3.6.4.13; 2681. DR PathwayCommons; Q9UMR2; -. DR SignaLink; Q9UMR2; -. DR BioGRID-ORCS; 11269; 196 hits in 1159 CRISPR screens. DR ChiTaRS; DDX19B; human. DR EvolutionaryTrace; Q9UMR2; -. DR GeneWiki; DDX19B; -. DR GenomeRNAi; 11269; -. DR Pharos; Q9UMR2; Tbio. DR PRO; PR:Q9UMR2; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9UMR2; Protein. DR Bgee; ENSG00000157349; Expressed in left testis and 122 other cell types or tissues. DR ExpressionAtlas; Q9UMR2; baseline and differential. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc. DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0004386; F:helicase activity; TAS:ProtInc. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central. DR GO; GO:0006406; P:mRNA export from nucleus; TAS:ProtInc. DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central. DR CDD; cd18787; SF2_C_DEAD; 1. DR DisProt; DP01560; -. DR Gene3D; 6.10.250.2170; -; 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; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1. DR PANTHER; PTHR47958:SF191; ATP-DEPENDENT RNA HELICASE DDX19B; 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; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. DR Genevisible; Q9UMR2; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm; KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; KW RNA-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..479 FT /note="ATP-dependent RNA helicase DDX19B" FT /id="PRO_0000055022" FT DOMAIN 125..295 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 306..474 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 2..300 FT /note="N-terminal lobe" FT REGION 34..54 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 55..68 FT /note="N-terminal helix" FT REGION 301..479 FT /note="C-terminal lobe" FT MOTIF 92..120 FT /note="Q motif" FT MOTIF 242..245 FT /note="DEAD box" FT BINDING 119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 138..145 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 429 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 432 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22223895" FT VAR_SEQ 1..109 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12219940, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_041347" FT VAR_SEQ 1..19 FT /note="MATDSWALAVDEQEAAAES -> MAGAAGRVQDRALRRFPITLPVGD (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044727" FT VAR_SEQ 100..130 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:11230166, FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4" FT /id="VSP_015239" FT VARIANT 149 FT /note="V -> L (in dbSNP:rs34607244)" FT /id="VAR_052160" FT MUTAGEN 223 FT /note="D->R: Impairs interaction with NUP214 and RNA." FT /evidence="ECO:0000269|PubMed:19219046" FT MUTAGEN 243 FT /note="E->Q: Loss of activity." FT /evidence="ECO:0000269|PubMed:10428971" FT MUTAGEN 258 FT /note="I->A: Impairs interaction with NUP214." FT /evidence="ECO:0000269|PubMed:19219046" FT MUTAGEN 259 FT /note="R->D: Impairs interaction with NUP214." FT /evidence="ECO:0000269|PubMed:19219046" FT MUTAGEN 262 FT /note="R->A: Impairs interaction with NUP214." FT /evidence="ECO:0000269|PubMed:19219046" FT CONFLICT 128 FT /note="A -> V (in Ref. 4; CAG33496)" FT /evidence="ECO:0000305" FT CONFLICT 201 FT /note="N -> Y (in Ref. 5; BAG63488)" FT /evidence="ECO:0000305" FT CONFLICT 331 FT /note="I -> T (in Ref. 4; CAG33496)" FT /evidence="ECO:0000305" FT CONFLICT 367 FT /note="M -> V (in Ref. 4; CAG38540)" FT /evidence="ECO:0000305" FT HELIX 56..66 FT /evidence="ECO:0007829|PDB:6B4K" FT HELIX 67..70 FT /evidence="ECO:0007829|PDB:3G0H" FT HELIX 76..80 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 82..86 FT /evidence="ECO:0007829|PDB:3EWS" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:6B4K" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 101..109 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 117..127 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 134..137 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 144..155 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 165..168 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 172..185 FT /evidence="ECO:0007829|PDB:3FHT" FT TURN 186..188 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 194..197 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 212..216 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 218..225 FT /evidence="ECO:0007829|PDB:3FHT" FT TURN 226..228 FT /evidence="ECO:0007829|PDB:6B4K" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 238..242 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 244..248 FT /evidence="ECO:0007829|PDB:3FHT" FT TURN 250..253 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 254..262 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 269..275 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 279..288 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 299..301 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:3EWS" FT STRAND 307..313 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 317..331 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 332..339 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 343..355 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 361..363 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 369..380 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 385..389 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 394..396 FT /evidence="ECO:0007829|PDB:3G0H" FT STRAND 402..409 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 414..418 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 420..427 FT /evidence="ECO:0007829|PDB:3FHT" FT STRAND 429..431 FT /evidence="ECO:0007829|PDB:6B4J" FT STRAND 437..443 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 446..459 FT /evidence="ECO:0007829|PDB:3FHT" FT HELIX 471..478 FT /evidence="ECO:0007829|PDB:6B4K" SQ SEQUENCE 479 AA; 53927 MW; 8F6F93B12B7E9871 CRC64; MATDSWALAV DEQEAAAESL SNLHLKEEKI KPDTNGAVVK TNANAEKTDE EEKEDRAAQS LLNKLIRSNL VDNTNQVEVL QRDPNSPLYS VKSFEELRLK PQLLQGVYAM GFNRPSKIQE NALPLMLAEP PQNLIAQSQS GTGKTAAFVL AMLSQVEPAN KYPQCLCLSP TYELALQTGK VIEQMGKFYP ELKLAYAVRG NKLERGQKIS EQIVIGTPGT VLDWCSKLKF IDPKKIKVFV LDEADVMIAT QGHQDQSIRI QRMLPRNCQM LLFSATFEDS VWKFAQKVVP DPNVIKLKRE EETLDTIKQY YVLCSSRDEK FQALCNLYGA ITIAQAMIFC HTRKTASWLA AELSKEGHQV ALLSGEMMVE QRAAVIERFR EGKEKVLVTT NVCARGIDVE QVSVVINFDL PVDKDGNPDN ETYLHRIGRT GRFGKRGLAV NMVDSKHSMN ILNRIQEHFN KKIERLDTDD LDEIEKIAN //