DD19B_HUMAN
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 03-AUG-2022, entry version 198.
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}.
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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; 307.
DR DIP; DIP-48486N; -.
DR IntAct; Q9UMR2; 101.
DR MINT; Q9UMR2; -.
DR STRING; 9606.ENSP00000288071; -.
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; Q9UMR2; -.
DR PeptideAtlas; Q9UMR2; -.
DR PRIDE; Q9UMR2; -.
DR ProteomicsDB; 16960; -.
DR ProteomicsDB; 85194; -. [Q9UMR2-1]
DR ProteomicsDB; 85195; -. [Q9UMR2-2]
DR ProteomicsDB; 85196; -. [Q9UMR2-3]
DR Antibodypedia; 16335; 334 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 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; EYCTPIQ; -.
DR OrthoDB; 608788at2759; -.
DR PhylomeDB; Q9UMR2; -.
DR TreeFam; TF314957; -.
DR BRENDA; 3.6.4.13; 2681.
DR PathwayCommons; Q9UMR2; -.
DR SignaLink; Q9UMR2; -.
DR BioGRID-ORCS; 11269; 193 hits in 1080 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 120 other tissues.
DR ExpressionAtlas; Q9UMR2; baseline and differential.
DR Genevisible; Q9UMR2; HS.
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 DisProt; DP01560; -.
DR Gene3D; 3.40.50.300; -; 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 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; 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; 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
