Full text data of DDX19B
DDX19B
(DBP5, DDX19, TDBP)
[Confidence: low (only semi-automatic identification from reviews)]
ATP-dependent RNA helicase DDX19B; 3.6.4.13 (DEAD box RNA helicase DEAD5; DEAD box protein 19B)
ATP-dependent RNA helicase DDX19B; 3.6.4.13 (DEAD box RNA helicase DEAD5; DEAD box protein 19B)
UniProt
Q9UMR2
ID DD19B_HUMAN Reviewed; 479 AA.
AC Q9UMR2; B3KNE9; B4DXS6; E7EMK4; Q6FIB7; Q6IAE0; Q96KE7; Q9H0U0;
read moreDT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=ATP-dependent RNA helicase DDX19B;
DE EC=3.6.4.13;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, AND
RP 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.,
RA Boscheron C., Rigaut G., Wilm M., Seraphin B., Carmo-Fonseca M.,
RA Izaurralde E.;
RT "Dbp5, a DEAD-box protein required for mRNA export, is recruited to
RT the cytoplasmic fibrils of nuclear pore complex via a conserved
RT interaction 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
RT of 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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.,
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 [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.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA 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.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 54-475 ALONE AND IN COMPLEX
RP WITH 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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 68-479 IN COMPLEX WITH NUP214
RP AND ATP ANALOG, ATP-BINDING SITES, AND MUTAGENESIS OF ASP-223;
RP ILE-258; ARG-259 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
RT nucleoporin NUP214 in a mutually exclusive manner.";
RL Nat. Struct. Mol. Biol. 16:247-254(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 1-300 IN COMPLEX WITH NUP214
RP AND ADP.
RX PubMed=19208808; DOI=10.1073/pnas.0813267106;
RA Napetschnig J., Kassube S.A., Debler E.W., Wong R.W., Blobel G.,
RA 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
CC the nucleus. Rather than unwinding RNA duplexes, DDX19B functions
CC as a remodeler of ribonucleoprotein particles, whereby proteins
CC bound to nuclear mRNA are dissociated and replaced by cytoplasmic
CC mRNA binding proteins.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Interacts with NUP214 or RNA in a mutually exclusive
CC manner.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nuclear pore complex.
CC Nucleus membrane; Peripheral membrane protein; Cytoplasmic side.
CC Note=Nuclear pore complex cytoplasmic fibrils.
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 Note=No experimental confirmation available;
CC -!- DOMAIN: The N-terminal extension helix acts as an autoinhibitory
CC domain, preventing ATP hydrolysis, unless the N-terminus of the
CC protein is displaced by RNA binding, allowing cleft closure to
CC bring key side chains into position for catalysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5
CC subfamily.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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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 RefSeq; NP_001014449.1; NM_001014449.2.
DR RefSeq; NP_001014451.1; NM_001014451.2.
DR RefSeq; NP_001244101.1; NM_001257172.1.
DR RefSeq; NP_001244102.1; NM_001257173.1.
DR RefSeq; NP_001244103.1; NM_001257174.1.
DR RefSeq; NP_009173.1; NM_007242.5.
DR UniGene; Hs.221761; -.
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 PDBsum; 3EWS; -.
DR PDBsum; 3FHC; -.
DR PDBsum; 3FHT; -.
DR PDBsum; 3FMO; -.
DR PDBsum; 3FMP; -.
DR PDBsum; 3G0H; -.
DR ProteinModelPortal; Q9UMR2; -.
DR SMR; Q9UMR2; 60-467.
DR DIP; DIP-48486N; -.
DR IntAct; Q9UMR2; 13.
DR MINT; MINT-4831823; -.
DR STRING; 9606.ENSP00000288071; -.
DR PhosphoSite; Q9UMR2; -.
DR DMDM; 10719979; -.
DR PaxDb; Q9UMR2; -.
DR PRIDE; Q9UMR2; -.
DR DNASU; 11269; -.
DR Ensembl; ENST00000288071; ENSP00000288071; ENSG00000157349.
DR Ensembl; ENST00000355992; ENSP00000348271; ENSG00000157349.
DR Ensembl; ENST00000393657; ENSP00000377267; ENSG00000157349.
DR Ensembl; ENST00000451014; ENSP00000392639; ENSG00000157349.
DR Ensembl; ENST00000563392; ENSP00000456574; ENSG00000157349.
DR Ensembl; ENST00000568625; ENSP00000456757; ENSG00000157349.
DR GeneID; 11269; -.
DR KEGG; hsa:11269; -.
DR UCSC; uc010vlv.3; human.
DR CTD; 11269; -.
DR GeneCards; GC16P070328; -.
DR HGNC; HGNC:2742; DDX19B.
DR HPA; CAB037284; -.
DR MIM; 605812; gene.
DR neXtProt; NX_Q9UMR2; -.
DR PharmGKB; PA27208; -.
DR eggNOG; COG0513; -.
DR HOGENOM; HOG000268797; -.
DR HOVERGEN; HBG107989; -.
DR InParanoid; Q9UMR2; -.
DR PhylomeDB; Q9UMR2; -.
DR ChiTaRS; DDX19B; human.
DR EvolutionaryTrace; Q9UMR2; -.
DR GeneWiki; DDX19B; -.
DR GenomeRNAi; 11269; -.
DR NextBio; 42879; -.
DR PRO; PR:Q9UMR2; -.
DR ArrayExpress; Q9UMR2; -.
DR Bgee; Q9UMR2; -.
DR CleanEx; HS_DDX19B; -.
DR Genevestigator; Q9UMR2; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0006406; P:mRNA export from nucleus; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
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;
KW Complete proteome; Cytoplasm; Helicase; Hydrolase; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleotide-binding; Nucleus;
KW Polymorphism; Protein transport; Reference proteome; RNA-binding;
KW Translocation; Transport.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 479 ATP-dependent RNA helicase DDX19B.
FT /FTId=PRO_0000055022.
FT DOMAIN 125 295 Helicase ATP-binding.
FT DOMAIN 306 474 Helicase C-terminal.
FT NP_BIND 138 145 ATP.
FT REGION 2 300 N-terminal lobe.
FT REGION 55 68 N-terminal helix.
FT REGION 301 479 C-terminal lobe.
FT MOTIF 92 120 Q motif.
FT MOTIF 242 245 DEAD box.
FT BINDING 119 119 ATP.
FT BINDING 429 429 ATP.
FT BINDING 432 432 ATP.
FT MOD_RES 2 2 N-acetylalanine (By similarity).
FT VAR_SEQ 1 109 Missing (in isoform 3).
FT /FTId=VSP_041347.
FT VAR_SEQ 1 19 MATDSWALAVDEQEAAAES -> MAGAAGRVQDRALRRFPI
FT TLPVGD (in isoform 4).
FT /FTId=VSP_044727.
FT VAR_SEQ 100 130 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_015239.
FT VARIANT 149 149 V -> L (in dbSNP:rs34607244).
FT /FTId=VAR_052160.
FT MUTAGEN 223 223 D->R: Impairs interaction with NUP214 and
FT RNA.
FT MUTAGEN 243 243 E->Q: Loss of activity.
FT MUTAGEN 258 258 I->A: Impairs interaction with NUP214.
FT MUTAGEN 259 259 R->D: Impairs interaction with NUP214.
FT MUTAGEN 262 262 R->A: Impairs interaction with NUP214.
FT CONFLICT 128 128 A -> V (in Ref. 4; CAG33496).
FT CONFLICT 201 201 N -> Y (in Ref. 5; BAG63488).
FT CONFLICT 331 331 I -> T (in Ref. 4; CAG33496).
FT CONFLICT 367 367 M -> V (in Ref. 4; CAG38540).
FT HELIX 56 66
FT HELIX 67 70
FT HELIX 76 80
FT STRAND 82 86
FT HELIX 95 97
FT HELIX 101 109
FT HELIX 117 127
FT STRAND 128 130
FT STRAND 134 137
FT HELIX 144 155
FT STRAND 165 168
FT HELIX 172 185
FT TURN 186 188
FT STRAND 194 197
FT STRAND 212 216
FT HELIX 218 225
FT TURN 226 228
FT HELIX 233 235
FT STRAND 238 242
FT HELIX 244 248
FT TURN 250 253
FT HELIX 254 262
FT STRAND 269 275
FT HELIX 279 288
FT STRAND 289 291
FT STRAND 293 295
FT HELIX 299 301
FT HELIX 304 306
FT STRAND 307 313
FT HELIX 317 331
FT STRAND 332 339
FT HELIX 343 355
FT STRAND 361 363
FT HELIX 369 380
FT STRAND 385 389
FT HELIX 391 393
FT STRAND 394 396
FT STRAND 402 409
FT STRAND 414 418
FT HELIX 420 427
FT STRAND 437 443
FT HELIX 446 459
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
//
ID DD19B_HUMAN Reviewed; 479 AA.
AC Q9UMR2; B3KNE9; B4DXS6; E7EMK4; Q6FIB7; Q6IAE0; Q96KE7; Q9H0U0;
read moreDT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=ATP-dependent RNA helicase DDX19B;
DE EC=3.6.4.13;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, AND
RP 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.,
RA Boscheron C., Rigaut G., Wilm M., Seraphin B., Carmo-Fonseca M.,
RA Izaurralde E.;
RT "Dbp5, a DEAD-box protein required for mRNA export, is recruited to
RT the cytoplasmic fibrils of nuclear pore complex via a conserved
RT interaction 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
RT of 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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.,
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 [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.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA 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.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 54-475 ALONE AND IN COMPLEX
RP WITH 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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 68-479 IN COMPLEX WITH NUP214
RP AND ATP ANALOG, ATP-BINDING SITES, AND MUTAGENESIS OF ASP-223;
RP ILE-258; ARG-259 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
RT nucleoporin NUP214 in a mutually exclusive manner.";
RL Nat. Struct. Mol. Biol. 16:247-254(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 1-300 IN COMPLEX WITH NUP214
RP AND ADP.
RX PubMed=19208808; DOI=10.1073/pnas.0813267106;
RA Napetschnig J., Kassube S.A., Debler E.W., Wong R.W., Blobel G.,
RA 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
CC the nucleus. Rather than unwinding RNA duplexes, DDX19B functions
CC as a remodeler of ribonucleoprotein particles, whereby proteins
CC bound to nuclear mRNA are dissociated and replaced by cytoplasmic
CC mRNA binding proteins.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Interacts with NUP214 or RNA in a mutually exclusive
CC manner.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nuclear pore complex.
CC Nucleus membrane; Peripheral membrane protein; Cytoplasmic side.
CC Note=Nuclear pore complex cytoplasmic fibrils.
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 Note=No experimental confirmation available;
CC -!- DOMAIN: The N-terminal extension helix acts as an autoinhibitory
CC domain, preventing ATP hydrolysis, unless the N-terminus of the
CC protein is displaced by RNA binding, allowing cleft closure to
CC bring key side chains into position for catalysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5
CC subfamily.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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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 RefSeq; NP_001014449.1; NM_001014449.2.
DR RefSeq; NP_001014451.1; NM_001014451.2.
DR RefSeq; NP_001244101.1; NM_001257172.1.
DR RefSeq; NP_001244102.1; NM_001257173.1.
DR RefSeq; NP_001244103.1; NM_001257174.1.
DR RefSeq; NP_009173.1; NM_007242.5.
DR UniGene; Hs.221761; -.
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 PDBsum; 3EWS; -.
DR PDBsum; 3FHC; -.
DR PDBsum; 3FHT; -.
DR PDBsum; 3FMO; -.
DR PDBsum; 3FMP; -.
DR PDBsum; 3G0H; -.
DR ProteinModelPortal; Q9UMR2; -.
DR SMR; Q9UMR2; 60-467.
DR DIP; DIP-48486N; -.
DR IntAct; Q9UMR2; 13.
DR MINT; MINT-4831823; -.
DR STRING; 9606.ENSP00000288071; -.
DR PhosphoSite; Q9UMR2; -.
DR DMDM; 10719979; -.
DR PaxDb; Q9UMR2; -.
DR PRIDE; Q9UMR2; -.
DR DNASU; 11269; -.
DR Ensembl; ENST00000288071; ENSP00000288071; ENSG00000157349.
DR Ensembl; ENST00000355992; ENSP00000348271; ENSG00000157349.
DR Ensembl; ENST00000393657; ENSP00000377267; ENSG00000157349.
DR Ensembl; ENST00000451014; ENSP00000392639; ENSG00000157349.
DR Ensembl; ENST00000563392; ENSP00000456574; ENSG00000157349.
DR Ensembl; ENST00000568625; ENSP00000456757; ENSG00000157349.
DR GeneID; 11269; -.
DR KEGG; hsa:11269; -.
DR UCSC; uc010vlv.3; human.
DR CTD; 11269; -.
DR GeneCards; GC16P070328; -.
DR HGNC; HGNC:2742; DDX19B.
DR HPA; CAB037284; -.
DR MIM; 605812; gene.
DR neXtProt; NX_Q9UMR2; -.
DR PharmGKB; PA27208; -.
DR eggNOG; COG0513; -.
DR HOGENOM; HOG000268797; -.
DR HOVERGEN; HBG107989; -.
DR InParanoid; Q9UMR2; -.
DR PhylomeDB; Q9UMR2; -.
DR ChiTaRS; DDX19B; human.
DR EvolutionaryTrace; Q9UMR2; -.
DR GeneWiki; DDX19B; -.
DR GenomeRNAi; 11269; -.
DR NextBio; 42879; -.
DR PRO; PR:Q9UMR2; -.
DR ArrayExpress; Q9UMR2; -.
DR Bgee; Q9UMR2; -.
DR CleanEx; HS_DDX19B; -.
DR Genevestigator; Q9UMR2; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0006406; P:mRNA export from nucleus; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
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;
KW Complete proteome; Cytoplasm; Helicase; Hydrolase; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleotide-binding; Nucleus;
KW Polymorphism; Protein transport; Reference proteome; RNA-binding;
KW Translocation; Transport.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 479 ATP-dependent RNA helicase DDX19B.
FT /FTId=PRO_0000055022.
FT DOMAIN 125 295 Helicase ATP-binding.
FT DOMAIN 306 474 Helicase C-terminal.
FT NP_BIND 138 145 ATP.
FT REGION 2 300 N-terminal lobe.
FT REGION 55 68 N-terminal helix.
FT REGION 301 479 C-terminal lobe.
FT MOTIF 92 120 Q motif.
FT MOTIF 242 245 DEAD box.
FT BINDING 119 119 ATP.
FT BINDING 429 429 ATP.
FT BINDING 432 432 ATP.
FT MOD_RES 2 2 N-acetylalanine (By similarity).
FT VAR_SEQ 1 109 Missing (in isoform 3).
FT /FTId=VSP_041347.
FT VAR_SEQ 1 19 MATDSWALAVDEQEAAAES -> MAGAAGRVQDRALRRFPI
FT TLPVGD (in isoform 4).
FT /FTId=VSP_044727.
FT VAR_SEQ 100 130 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_015239.
FT VARIANT 149 149 V -> L (in dbSNP:rs34607244).
FT /FTId=VAR_052160.
FT MUTAGEN 223 223 D->R: Impairs interaction with NUP214 and
FT RNA.
FT MUTAGEN 243 243 E->Q: Loss of activity.
FT MUTAGEN 258 258 I->A: Impairs interaction with NUP214.
FT MUTAGEN 259 259 R->D: Impairs interaction with NUP214.
FT MUTAGEN 262 262 R->A: Impairs interaction with NUP214.
FT CONFLICT 128 128 A -> V (in Ref. 4; CAG33496).
FT CONFLICT 201 201 N -> Y (in Ref. 5; BAG63488).
FT CONFLICT 331 331 I -> T (in Ref. 4; CAG33496).
FT CONFLICT 367 367 M -> V (in Ref. 4; CAG38540).
FT HELIX 56 66
FT HELIX 67 70
FT HELIX 76 80
FT STRAND 82 86
FT HELIX 95 97
FT HELIX 101 109
FT HELIX 117 127
FT STRAND 128 130
FT STRAND 134 137
FT HELIX 144 155
FT STRAND 165 168
FT HELIX 172 185
FT TURN 186 188
FT STRAND 194 197
FT STRAND 212 216
FT HELIX 218 225
FT TURN 226 228
FT HELIX 233 235
FT STRAND 238 242
FT HELIX 244 248
FT TURN 250 253
FT HELIX 254 262
FT STRAND 269 275
FT HELIX 279 288
FT STRAND 289 291
FT STRAND 293 295
FT HELIX 299 301
FT HELIX 304 306
FT STRAND 307 313
FT HELIX 317 331
FT STRAND 332 339
FT HELIX 343 355
FT STRAND 361 363
FT HELIX 369 380
FT STRAND 385 389
FT HELIX 391 393
FT STRAND 394 396
FT STRAND 402 409
FT STRAND 414 418
FT HELIX 420 427
FT STRAND 437 443
FT HELIX 446 459
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
//
MIM
605812
*RECORD*
*FIELD* NO
605812
*FIELD* TI
*605812 DEAD/H BOX 19; DDX19
;;DBP5, YEAST, HOMOLOG OF; DBP5
*FIELD* TX
DESCRIPTION
read more
DEAD box proteins (e.g., EIF4A1; 602641) are members of the RNA helicase
protein family of RNA-dependent nucleotide triphosphatases. Dbp5 is a
DEAD box protein that plays an essential role in mRNA export from the
nucleus in yeast (Schmitt et al., 1999).
CLONING
By EST database searching and RT-PCR, Schmitt et al. (1999) obtained a
cDNA encoding DDX19, the human homolog of Dbp5. The deduced 479-amino
acid protein is 94% and 46% identical to the mouse and yeast sequences,
respectively. Western blot analysis showed that recombinant and native
proteins have an identical molecular mass of approximately 56 kD.
Functional analysis indicated that DDX19 exhibits RNA-dependent ATPase
and ATP-dependent RNA-unwinding activities. Fluorescence microscopy
demonstrated cytoplasmic expression of DDX19, with a fraction localized
at the nuclear rim. Tandem affinity purification analysis determined
that DDX19 interacts with an N-terminal sequence of the nucleoporin
CAN/Nup159p (NUP214; 114350). Immunoelectron microscopy revealed DDX19
localization at the cytoplasmic fibrils of the nuclear pore complex
(NPC). Mutational analysis established that glu243 in the DEAD box motif
is essential for RNA-dependent ATPase and unwinding activities and for
mRNA export. Schmitt et al. (1999) concluded that DDX19 is recruited to
the cytoplasmic fibrils of the NPC, where it participates in the export
of mRNA from the nucleus.
GENE FUNCTION
Using Saccharomyces cerevisiae as a model organism, Gross et al. (2007)
identified the DEAD box RNA helicase and mRNA export factor Dbp5 as a
player in translation termination. Dbp5 interacts genetically with both
release factors Erf1 (600285) and Erf3 (see 139259) and with the
polyadenylate-binding protein Pab1 (604679). A physical interaction was
specifically detected with eRF1. Moreover, Gross et al. (2007) showed
that the helicase activity of Dbp5 is required for efficient stop codon
recognition, and intact Dbp5 is essential for recruitment of eRF3 into
termination complexes. Therefore, Dbp5 controls the eRF3-eRF1
interaction and thus eRF3-mediated downstream events.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DDX19
gene to chromosome 16 (TMAP WI-16772).
*FIELD* RF
1. Gross, T.; Siepmann, A.; Sturm, D.; Windgassen, M.; Scarcelli,
J. J.; Seedorf, M.; Cole, C. N.; Krebber, H.: The DEAD-box RNA helicase
Dbp5 functions in translation termination. Science 315: 646-649,
2007.
2. Schmitt, C.; von Kobbe, C.; Bachi, A.; Pante, N.; Rodrigues, J.
P.; Boscheron, C.; Rigaut, G.; Wilm, M.; Seraphin, B.; Carmo-Fonseca,
M.; Izaurralde, E.: Dbp5, a DEAD-box protein required for mRNA export,
is recruited to the cytoplasmic fibrils of nuclear pore complex via
a conserved interaction with CAN/Nup159p. EMBO J. 18: 4332-4347,
1999.
*FIELD* CN
Ada Hamosh - updated: 4/25/2007
*FIELD* CD
Paul J. Converse: 4/3/2001
*FIELD* ED
alopez: 07/16/2009
carol: 6/15/2007
alopez: 5/1/2007
terry: 4/25/2007
mgross: 4/3/2001
*RECORD*
*FIELD* NO
605812
*FIELD* TI
*605812 DEAD/H BOX 19; DDX19
;;DBP5, YEAST, HOMOLOG OF; DBP5
*FIELD* TX
DESCRIPTION
read more
DEAD box proteins (e.g., EIF4A1; 602641) are members of the RNA helicase
protein family of RNA-dependent nucleotide triphosphatases. Dbp5 is a
DEAD box protein that plays an essential role in mRNA export from the
nucleus in yeast (Schmitt et al., 1999).
CLONING
By EST database searching and RT-PCR, Schmitt et al. (1999) obtained a
cDNA encoding DDX19, the human homolog of Dbp5. The deduced 479-amino
acid protein is 94% and 46% identical to the mouse and yeast sequences,
respectively. Western blot analysis showed that recombinant and native
proteins have an identical molecular mass of approximately 56 kD.
Functional analysis indicated that DDX19 exhibits RNA-dependent ATPase
and ATP-dependent RNA-unwinding activities. Fluorescence microscopy
demonstrated cytoplasmic expression of DDX19, with a fraction localized
at the nuclear rim. Tandem affinity purification analysis determined
that DDX19 interacts with an N-terminal sequence of the nucleoporin
CAN/Nup159p (NUP214; 114350). Immunoelectron microscopy revealed DDX19
localization at the cytoplasmic fibrils of the nuclear pore complex
(NPC). Mutational analysis established that glu243 in the DEAD box motif
is essential for RNA-dependent ATPase and unwinding activities and for
mRNA export. Schmitt et al. (1999) concluded that DDX19 is recruited to
the cytoplasmic fibrils of the NPC, where it participates in the export
of mRNA from the nucleus.
GENE FUNCTION
Using Saccharomyces cerevisiae as a model organism, Gross et al. (2007)
identified the DEAD box RNA helicase and mRNA export factor Dbp5 as a
player in translation termination. Dbp5 interacts genetically with both
release factors Erf1 (600285) and Erf3 (see 139259) and with the
polyadenylate-binding protein Pab1 (604679). A physical interaction was
specifically detected with eRF1. Moreover, Gross et al. (2007) showed
that the helicase activity of Dbp5 is required for efficient stop codon
recognition, and intact Dbp5 is essential for recruitment of eRF3 into
termination complexes. Therefore, Dbp5 controls the eRF3-eRF1
interaction and thus eRF3-mediated downstream events.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DDX19
gene to chromosome 16 (TMAP WI-16772).
*FIELD* RF
1. Gross, T.; Siepmann, A.; Sturm, D.; Windgassen, M.; Scarcelli,
J. J.; Seedorf, M.; Cole, C. N.; Krebber, H.: The DEAD-box RNA helicase
Dbp5 functions in translation termination. Science 315: 646-649,
2007.
2. Schmitt, C.; von Kobbe, C.; Bachi, A.; Pante, N.; Rodrigues, J.
P.; Boscheron, C.; Rigaut, G.; Wilm, M.; Seraphin, B.; Carmo-Fonseca,
M.; Izaurralde, E.: Dbp5, a DEAD-box protein required for mRNA export,
is recruited to the cytoplasmic fibrils of nuclear pore complex via
a conserved interaction with CAN/Nup159p. EMBO J. 18: 4332-4347,
1999.
*FIELD* CN
Ada Hamosh - updated: 4/25/2007
*FIELD* CD
Paul J. Converse: 4/3/2001
*FIELD* ED
alopez: 07/16/2009
carol: 6/15/2007
alopez: 5/1/2007
terry: 4/25/2007
mgross: 4/3/2001