DDX47_HUMAN
ID DDX47_HUMAN Reviewed; 455 AA.
AC Q9H0S4; B3KXP4; G5E955; Q96GM0; Q96NV8; Q9UI98;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX47;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 47;
GN Name=DDX47;
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 [LARGE SCALE MRNA] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Eye;
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 [6]
RP PROTEIN SEQUENCE OF 2-24; 75-102; 142-161; 170-190; 238-248; 285-301;
RP 315-325; 378-384 AND 424-441, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-455 (ISOFORM 2).
RC TISSUE=Liver;
RA Yu Y., Zhang C., Luo L., Ouyang S., Zhang S., Li W., Wu J., Zhou S.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 50 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP FUNCTION, INTERACTION WITH GABARAP, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15977068; DOI=10.1007/s10529-005-3628-2;
RA Lee J.H., Rho S.B., Chun T.;
RT "GABAA receptor-associated protein (GABARAP) induces apoptosis by
RT interacting with DEAD (Asp-Glu-Ala-Asp/His) box polypeptide 47 (DDX 47).";
RL Biotechnol. Lett. 27:623-628(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP FUNCTION, INTERACTION WITH NOL8, AND SUBCELLULAR LOCATION.
RX PubMed=16963496; DOI=10.1093/nar/gkl603;
RA Sekiguchi T., Hayano T., Yanagida M., Takahashi N., Nishimoto T.;
RT "NOP132 is required for proper nucleolus localization of DEAD-box RNA
RT helicase DDX47.";
RL Nucleic Acids Res. 34:4593-4608(2006).
RN [12]
RP INTERACTION WITH AGO1 AND AGO2.
RX PubMed=17932509; DOI=10.1038/sj.embor.7401088;
RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
RA Urlaub H., Meister G.;
RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein
RT complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP 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=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
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].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-9, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND THR-149, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-230 IN COMPLEX WITH AMP.
RX PubMed=20941364; DOI=10.1371/journal.pone.0012791;
RA Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L., Hogbom M.,
RA Holmberg-Schiavone L., Tempel W., Park H.W., Hammarstrom M., Moche M.,
RA Thorsell A.G., Schuler H.;
RT "Comparative structural analysis of human DEAD-box RNA helicases.";
RL PLoS ONE 5:E12791-E12791(2010).
RN [20]
RP VARIANTS TYR-8 AND GLU-107, AND TISSUE SPECIFICITY.
RX PubMed=31256877; DOI=10.1016/j.ajhg.2019.06.001;
RG University of Washington Center for Mendelian Genomics, Baylor-Hopkins Center for Mendelian Genomics, Telethon Undiagnosed Diseases Program;
RA Paine I., Posey J.E., Grochowski C.M., Jhangiani S.N., Rosenheck S.,
RA Kleyner R., Marmorale T., Yoon M., Wang K., Robison R., Cappuccio G.,
RA Pinelli M., Magli A., Coban Akdemir Z., Hui J., Yeung W.L., Wong B.K.Y.,
RA Ortega L., Bekheirnia M.R., Bierhals T., Hempel M., Johannsen J.,
RA Santer R., Aktas D., Alikasifoglu M., Bozdogan S., Aydin H., Karaca E.,
RA Bayram Y., Ityel H., Dorschner M., White J.J., Wilichowski E.,
RA Wortmann S.B., Casella E.B., Kitajima J.P., Kok F., Monteiro F.,
RA Muzny D.M., Bamshad M., Gibbs R.A., Sutton V.R., Van Esch H.,
RA Brunetti-Pierri N., Hildebrandt F., Brautbar A., Van den Veyver I.B.,
RA Glass I., Lessel D., Lyon G.J., Lupski J.R.;
RT "Paralog studies augment gene discovery: DDX and DHX genes.";
RL Am. J. Hum. Genet. 105:302-316(2019).
CC -!- FUNCTION: Involved in apoptosis. May have a role in rRNA processing and
CC mRNA splicing. Associates with pre-rRNA precursors.
CC {ECO:0000269|PubMed:15977068, ECO:0000269|PubMed:16963496}.
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: Interacts with AGO1 and AGO2. Interacts with GABARAP.
CC Interacts with NOL8; the interaction is RNA-dependent.
CC {ECO:0000269|PubMed:15977068, ECO:0000269|PubMed:16963496,
CC ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:20941364}.
CC -!- INTERACTION:
CC Q9H0S4; O95166: GABARAP; NbExp=3; IntAct=EBI-2515241, EBI-712001;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:16963496}. Note=Localizes in the nucleolar-
CC organizing region during ribosome biogenesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H0S4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0S4-2; Sequence=VSP_045239;
CC -!- TISSUE SPECIFICITY: Expressed in skin, lung and breast. Also expressed
CC in the brain. {ECO:0000269|PubMed:31256877}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF23354.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL136666; CAB66601.1; -; mRNA.
DR EMBL; AK054574; BAB70762.1; -; mRNA.
DR EMBL; AK127712; BAG54556.1; -; mRNA.
DR EMBL; AC007215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96277.1; -; Genomic_DNA.
DR EMBL; CH471094; EAW96283.1; -; Genomic_DNA.
DR EMBL; BC009379; AAH09379.2; -; mRNA.
DR EMBL; BC068009; AAH68009.1; -; mRNA.
DR EMBL; AF078843; AAF23354.1; ALT_INIT; mRNA.
DR CCDS; CCDS8655.1; -. [Q9H0S4-1]
DR CCDS; CCDS8656.1; -. [Q9H0S4-2]
DR RefSeq; NP_057439.2; NM_016355.3. [Q9H0S4-1]
DR RefSeq; NP_957518.1; NM_201224.1. [Q9H0S4-2]
DR PDB; 3BER; X-ray; 1.40 A; A=5-230.
DR PDBsum; 3BER; -.
DR AlphaFoldDB; Q9H0S4; -.
DR SMR; Q9H0S4; -.
DR BioGRID; 119375; 146.
DR IntAct; Q9H0S4; 54.
DR MINT; Q9H0S4; -.
DR STRING; 9606.ENSP00000350698; -.
DR GlyGen; Q9H0S4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H0S4; -.
DR MetOSite; Q9H0S4; -.
DR PhosphoSitePlus; Q9H0S4; -.
DR SwissPalm; Q9H0S4; -.
DR BioMuta; DDX47; -.
DR DMDM; 52782792; -.
DR SWISS-2DPAGE; Q9H0S4; -.
DR EPD; Q9H0S4; -.
DR jPOST; Q9H0S4; -.
DR MassIVE; Q9H0S4; -.
DR MaxQB; Q9H0S4; -.
DR PaxDb; Q9H0S4; -.
DR PeptideAtlas; Q9H0S4; -.
DR PRIDE; Q9H0S4; -.
DR ProteomicsDB; 33835; -.
DR ProteomicsDB; 80322; -. [Q9H0S4-1]
DR Antibodypedia; 3114; 201 antibodies from 25 providers.
DR DNASU; 51202; -.
DR Ensembl; ENST00000352940.8; ENSP00000319578.6; ENSG00000213782.7. [Q9H0S4-2]
DR Ensembl; ENST00000358007.7; ENSP00000350698.3; ENSG00000213782.7. [Q9H0S4-1]
DR GeneID; 51202; -.
DR KEGG; hsa:51202; -.
DR MANE-Select; ENST00000358007.7; ENSP00000350698.3; NM_016355.4; NP_057439.2.
DR UCSC; uc001rax.4; human. [Q9H0S4-1]
DR CTD; 51202; -.
DR GeneCards; DDX47; -.
DR HGNC; HGNC:18682; DDX47.
DR HPA; ENSG00000213782; Low tissue specificity.
DR MIM; 615428; gene.
DR neXtProt; NX_Q9H0S4; -.
DR OpenTargets; ENSG00000213782; -.
DR PharmGKB; PA134918403; -.
DR VEuPathDB; HostDB:ENSG00000213782; -.
DR eggNOG; KOG0330; Eukaryota.
DR GeneTree; ENSGT00940000155774; -.
DR HOGENOM; CLU_003041_1_1_1; -.
DR InParanoid; Q9H0S4; -.
DR OMA; YDIELYQ; -.
DR PhylomeDB; Q9H0S4; -.
DR TreeFam; TF105714; -.
DR PathwayCommons; Q9H0S4; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9H0S4; -.
DR BioGRID-ORCS; 51202; 778 hits in 1076 CRISPR screens.
DR ChiTaRS; DDX47; human.
DR EvolutionaryTrace; Q9H0S4; -.
DR GeneWiki; DDX47; -.
DR GenomeRNAi; 51202; -.
DR Pharos; Q9H0S4; Tbio.
DR PRO; PR:Q9H0S4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H0S4; protein.
DR Bgee; ENSG00000213782; Expressed in islet of Langerhans and 98 other tissues.
DR ExpressionAtlas; Q9H0S4; baseline and differential.
DR Genevisible; Q9H0S4; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR CDD; cd17954; DEADc_DDX47; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR044765; DDX47/Rrp3_DEADc.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; ATP-binding;
KW Direct protein sequencing; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; rRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CHAIN 2..455
FT /note="Probable ATP-dependent RNA helicase DDX47"
FT /id="PRO_0000055050"
FT DOMAIN 55..226
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 237..397
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 24..52
FT /note="Q motif"
FT MOTIF 174..177
FT /note="DEAD box"
FT COMPBIAS 413..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 149
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 251..299
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_045239"
FT VARIANT 8
FT /note="D -> Y (found in a patient with a neurodevelopmental
FT disorder; unknown pathological significance;
FT dbSNP:rs577622688)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083613"
FT VARIANT 107
FT /note="Q -> E (found in a patient with a neurodevelopmental
FT disorder; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083614"
FT CONFLICT 55
FT /note="I -> V (in Ref. 3; BAB70762)"
FT /evidence="ECO:0000305"
FT HELIX 18..23
FT /evidence="ECO:0007829|PDB:3BER"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:3BER"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:3BER"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:3BER"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3BER"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:3BER"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:3BER"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:3BER"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3BER"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:3BER"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:3BER"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:3BER"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:3BER"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:3BER"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:3BER"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:3BER"
FT STRAND 197..207
FT /evidence="ECO:0007829|PDB:3BER"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:3BER"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:3BER"
SQ SEQUENCE 455 AA; 50647 MW; 5F64F26AD2C11286 CRC64;
MAAPEEHDSP TEASQPIVEE EETKTFKDLG VTDVLCEACD QLGWTKPTKI QIEAIPLALQ
GRDIIGLAET GSGKTGAFAL PILNALLETP QRLFALVLTP TRELAFQISE QFEALGSSIG
VQSAVIVGGI DSMSQSLALA KKPHIIIATP GRLIDHLENT KGFNLRALKY LVMDEADRIL
NMDFETEVDK ILKVIPRDRK TFLFSATMTK KVQKLQRAAL KNPVKCAVSS KYQTVEKLQQ
YYIFIPSKFK DTYLVYILNE LAGNSFMIFC STCNNTQRTA LLLRNLGFTA IPLHGQMSQS
KRLGSLNKFK AKARSILLAT DVASRGLDIP HVDVVVNFDI PTHSKDYIHR VGRTARAGRS
GKAITFVTQY DVELFQRIEH LIGKKLPGFP TQDDEVMMLT ERVAEAQRFA RMELREHGEK
KKRSREDAGD NDDTEGAIGV RNKVAGGKMK KRKGR
