ID DDX42_HUMAN Reviewed; 938 AA. AC Q86XP3; A6NML1; A8KA43; O75619; Q68G51; Q96BK1; Q96HR7; Q9Y3V8; DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 02-SEP-2026, entry version 189. DE RecName: Full=ATP-dependent RNA helicase DDX42; DE EC=3.6.4.13 {ECO:0000269|PubMed:16397294}; DE AltName: Full=DEAD box protein 42; DE AltName: Full=RNA helicase-like protein {ECO:0000303|PubMed:10727850}; DE Short=RHELP {ECO:0000303|PubMed:10727850}; DE AltName: Full=RNA helicase-related protein {ECO:0000303|Ref.2}; DE Short=RNAHP; DE AltName: Full=SF3b DEAD box protein; DE AltName: Full=Splicing factor 3B-associated 125 kDa protein {ECO:0000303|PubMed:12234937}; DE Short=SF3b125 {ECO:0000303|PubMed:12234937}; GN Name=DDX42 {ECO:0000303|PubMed:16397294, ECO:0000312|HGNC:HGNC:18676}; 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 2), AND TISSUE SPECIFICITY. RX PubMed=10727850; DOI=10.1016/s0925-4439(00)00010-7; RA Suk K., Kim S., Kim Y.-H., Oh S.-H., Lee M.-K., Kim K.-W., Kim H.-D., RA Seo Y.-S., Lee M.-S.; RT "Identification of a novel human member of the DEAD box protein family."; RL Biochim. Biophys. Acta 1501:63-69(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Ikeda A., Tsuritani K.; RT "Expression of RNA helicase-related protein in human hair follicle."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Trachea; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Eye, Pancreas, and Uterus; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 574-938 (ISOFORMS 1/2). RC TISSUE=Uterus; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 2), SUBCELLULAR LOCATION, AND RP IDENTIFICATION IN THE SF3B COMPLEX. RX PubMed=12234937; DOI=10.1093/emboj/cdf480; RA Will C.L., Urlaub H., Achsel T., Gentzel M., Wilm M., Luehrmann R.; RT "Characterization of novel SF3b and 17S U2 snRNP proteins, including a RT human Prp5p homologue and an SF3b DEAD-box protein."; RL EMBO J. 21:4978-4988(2002). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, AND 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 [10] RP FUNCTION, CATALYTIC ACTIVITY, RNA-BINDING, TISSUE SPECIFICITY, AND RP SUBCELLULAR LOCATION. RX PubMed=16397294; DOI=10.1093/nar/gkj403; RA Uhlmann-Schiffler H., Jalal C., Stahl H.; RT "Ddx42p -- a human DEAD box protein with RNA chaperone activities."; RL Nucleic Acids Res. 34:10-22(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-109; SER-111; RP SER-185 AND SER-754, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [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 [13] RP FUNCTION, INTERACTION WITH TP53BP2, AND SUBCELLULAR LOCATION. RX PubMed=19377511; DOI=10.1038/onc.2009.75; RA Uhlmann-Schiffler H., Kiermayer S., Stahl H.; RT "The DEAD box protein Ddx42p modulates the function of ASPP2, a stimulator RT of apoptosis."; RL Oncogene 28:2065-2073(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, AND RP IDENTIFICATION BY MASS SPECTROMETRY [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 [17] 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 [18] RP 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-185 AND SER-754, 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-12, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-899, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [23] {ECO:0007744|PDB:8HK1} RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS) IN COMPLEX WITH THE 17S RP U2 SNRNP COMPLEX, FUNCTION, AND IDENTIFICATION IN THE 17S U2 SNRNP COMPLEX. RX PubMed=36797247; DOI=10.1038/s41467-023-36489-x; RA Yang F., Bian T., Zhan X., Chen Z., Xing Z., Larsen N.A., Zhang X., Shi Y.; RT "Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP RT assembly."; RL Nat. Commun. 14:897-897(2023). CC -!- FUNCTION: ATP-dependent RNA helicase that binds to partially double- CC stranded RNAs (dsRNAs) in order to unwind RNA secondary structures CC (PubMed:16397294). Unwinding is promoted in the presence of single- CC strand binding proteins (PubMed:16397294). Also mediates RNA duplex CC formation thereby displacing the single-strand RNA binding protein CC (PubMed:16397294). ATP and ADP modulate its activity: ATP binding and CC hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP- CC bound form of the protein triggers annealing of complementary RNA CC strands (PubMed:16397294). Required for assembly of the 17S U2 SnRNP CC complex of the spliceosome, a large ribonucleoprotein complex that CC removes introns from transcribed pre-mRNAs: DDX42 associates CC transiently with the SF3B subcomplex of the 17S U2 SnRNP complex and is CC released after fulfilling its role in the assembly of 17S U2 SnRNP CC (PubMed:12234937, PubMed:36797247). Involved in the survival of cells CC by interacting with TP53BP2 and thereby counteracting the apoptosis- CC stimulating activity of TP53BP2 (PubMed:19377511). Relocalizes TP53BP2 CC to the cytoplasm (PubMed:19377511). {ECO:0000269|PubMed:12234937, CC ECO:0000269|PubMed:16397294, ECO:0000269|PubMed:19377511, CC ECO:0000269|PubMed:36797247}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); 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:16397294}; CC -!- SUBUNIT: Transient component of the SF3B subcomplex of the 17S U2 SnRNP CC complex (PubMed:12234937, PubMed:36797247). Interacts (via the C- CC terminus) with TP53BP2; the interaction is not inhibited by TP53BP2 CC ubiquitination and is independent of p53/TP53 (PubMed:19377511). CC {ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:19377511, CC ECO:0000269|PubMed:36797247}. CC -!- INTERACTION: CC Q86XP3; Q15428: SF3A2; NbExp=2; IntAct=EBI-722353, EBI-2462271; CC Q86XP3; Q15427: SF3B4; NbExp=3; IntAct=EBI-722353, EBI-348469; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19377511}. Nucleus CC {ECO:0000269|PubMed:16397294, ECO:0000269|PubMed:19377511}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, Cajal body CC {ECO:0000269|PubMed:12234937}. Nucleus speckle CC {ECO:0000269|PubMed:12234937}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q86XP3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q86XP3-2; Sequence=VSP_023518; CC -!- TISSUE SPECIFICITY: Expressed in several cell lines (at protein level). CC Expressed in liver, lung, tonsil, thymus, muscle and pancreatic islets. CC {ECO:0000269|PubMed:10727850, ECO:0000269|PubMed:16397294}. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX42 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC32396.1; Type=Frameshift; Evidence={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; AF083255; AAC32396.1; ALT_FRAME; mRNA. DR EMBL; AB036090; BAC66466.1; -; mRNA. DR EMBL; AK292908; BAF85597.1; -; mRNA. DR EMBL; AC015651; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471109; EAW94277.1; -; Genomic_DNA. DR EMBL; BC008208; AAH08208.1; -; mRNA. DR EMBL; BC015505; AAH15505.1; -; mRNA. DR EMBL; BC078667; AAH78667.1; -; mRNA. DR EMBL; BC093081; AAH93081.1; -; mRNA. DR EMBL; AL050096; CAB43268.1; -; mRNA. DR EMBL; BK000566; DAA00077.1; -; mRNA. DR CCDS; CCDS32704.1; -. [Q86XP3-1] DR PIR; T08745; T08745. DR RefSeq; NP_031398.2; NM_007372.3. [Q86XP3-1] DR RefSeq; NP_987095.1; NM_203499.3. [Q86XP3-1] DR RefSeq; XP_047291237.1; XM_047435281.1. [Q86XP3-1] DR RefSeq; XP_047291238.1; XM_047435282.1. [Q86XP3-1] DR RefSeq; XP_054170905.1; XM_054314930.1. [Q86XP3-1] DR RefSeq; XP_054170906.1; XM_054314931.1. [Q86XP3-1] DR PDB; 7EVN; EM; 2.60 A; E=1-938. DR PDB; 8DPE; X-ray; 1.53 A; A=211-646. DR PDB; 8HK1; EM; 2.70 A; E=1-938. DR AlphaFoldDB; Q86XP3; -. DR EMDB; EMD-31330; -. DR EMDB; EMD-34841; -. DR SMR; Q86XP3; -. DR BioGRID; 116454; 235. DR CORUM; Q86XP3; -. DR FunCoup; Q86XP3; 5607. DR IntAct; Q86XP3; 99. DR MINT; Q86XP3; -. DR NDEx; MUSIC2-C5189-DDX42; Osteosarcoma (U2OS) cell map - Pre-mRNA splicing and ribonucleoprotein assembly (49 proteins). DR STRING; 9606.ENSP00000464050; -. DR BindingDB; Q86XP3; -. DR ChEMBL; CHEMBL4105782; -. DR GlyCosmos; Q86XP3; 2 sites, 1 glycan. DR GlyGen; Q86XP3; 14 sites, 1 O-linked glycan (14 sites). DR iPTMnet; Q86XP3; -. DR MetOSite; Q86XP3; -. DR PhosphoSitePlus; Q86XP3; -. DR SwissPalm; Q86XP3; -. DR BioMuta; DDX42; -. DR DMDM; 74750541; -. DR jPOST; Q86XP3; -. DR MassIVE; Q86XP3; -. DR PaxDb; 9606-ENSP00000464050; -. DR PeptideAtlas; Q86XP3; -. DR ProteomicsDB; 70312; -. [Q86XP3-1] DR ProteomicsDB; 70313; -. [Q86XP3-2] DR Pumba; Q86XP3; -. DR Antibodypedia; 18710; 97 antibodies from 20 providers. DR DNASU; 11325; -. DR Ensembl; ENST00000359353.9; ENSP00000352308.5; ENSG00000198231.15. [Q86XP3-2] DR Ensembl; ENST00000389924.7; ENSP00000374574.2; ENSG00000198231.15. [Q86XP3-1] DR Ensembl; ENST00000578681.5; ENSP00000464050.1; ENSG00000198231.15. [Q86XP3-1] DR Ensembl; ENST00000583590.5; ENSP00000463561.1; ENSG00000198231.15. [Q86XP3-1] DR Ensembl; ENST00000878522.1; ENSP00000548581.1; ENSG00000198231.15. [Q86XP3-1] DR Ensembl; ENST00000878523.1; ENSP00000548582.1; ENSG00000198231.15. [Q86XP3-1] DR Ensembl; ENST00000878524.1; ENSP00000548583.1; ENSG00000198231.15. [Q86XP3-1] DR Ensembl; ENST00000878525.1; ENSP00000548584.1; ENSG00000198231.15. [Q86XP3-1] DR Ensembl; ENST00000878526.1; ENSP00000548585.1; ENSG00000198231.15. [Q86XP3-1] DR Ensembl; ENST00000878527.1; ENSP00000548586.1; ENSG00000198231.15. [Q86XP3-1] DR Ensembl; ENST00000927681.1; ENSP00000597740.1; ENSG00000198231.15. [Q86XP3-1] DR Ensembl; ENST00000927682.1; ENSP00000597741.1; ENSG00000198231.15. [Q86XP3-1] DR Ensembl; ENST00000927683.1; ENSP00000597742.1; ENSG00000198231.15. [Q86XP3-1] DR Ensembl; ENST00000927684.1; ENSP00000597743.1; ENSG00000198231.15. [Q86XP3-1] DR Ensembl; ENST00000927685.1; ENSP00000597744.1; ENSG00000198231.15. [Q86XP3-1] DR Ensembl; ENST00000960536.1; ENSP00000630595.1; ENSG00000198231.15. [Q86XP3-1] DR GeneID; 11325; -. DR KEGG; hsa:11325; -. DR MANE-Select; ENST00000389924.7; ENSP00000374574.2; NM_203499.3; NP_987095.1. DR UCSC; uc002jbu.5; human. [Q86XP3-1] DR AGR; HGNC:18676; -. DR ClinPGx; PA134875761; -. DR CTD; 11325; -. DR DisGeNET; 11325; -. DR GeneCards; DDX42; -. DR HGNC; HGNC:18676; DDX42. DR HPA; ENSG00000198231; Low tissue specificity. DR MIM; 613369; gene. DR OpenTargets; ENSG00000198231; -. DR VEuPathDB; HostDB:ENSG00000198231; -. DR eggNOG; KOG0339; Eukaryota. DR GeneTree; ENSGT00940000156559; -. DR InParanoid; Q86XP3; -. DR OMA; DHTWEQT; -. DR OrthoDB; 196131at2759; -. DR PAN-GO; Q86XP3; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q86XP3; -. DR PathwayCommons; Q86XP3; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway. DR Reactome; R-HSA-9770562; mRNA Polyadenylation. DR Reactome; R-HSA-9918481; Dengue Virus-Host Interactions. DR Reactome; R-HSA-9943411; CHD1 and CHD2 subfamily. DR SignaLink; Q86XP3; -. DR Agora; ENSG00000198231; -. DR BioGRID-ORCS; 11325; 535 hits in 1174 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR ChiTaRS; DDX42; human. DR GeneWiki; DDX42; -. DR GenomeRNAi; 11325; -. DR Pharos; Q86XP3; Tchem. DR PRO; PR:Q86XP3; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q86XP3; protein. DR Bgee; ENSG00000198231; Expressed in body of pancreas and 205 other cell types or tissues. DR ExpressionAtlas; Q86XP3; baseline and differential. DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0071004; C:U2-type prespliceosome; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; EXP:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:FlyBase. DR GO; GO:0003724; F:RNA helicase activity; IDA:FlyBase. DR GO; GO:0008104; P:intracellular protein localization; IDA:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:1903241; P:U2-type prespliceosome assembly; IDA:UniProtKB. DR CDD; cd17952; DEADc_DDX42; 1. DR CDD; cd18787; SF2_C_DEAD; 1. DR FunFam; 3.40.50.300:FF:000524; ATP-dependent RNA helicase DDX42; 1. DR FunFam; 3.40.50.300:FF:000079; probable ATP-dependent RNA helicase DDX17; 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-like. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 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; 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. DR PDBsum; 7EVN; -. DR PDBsum; 8DPE; -. DR PDBsum; 8HK1; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Coiled coil; KW Cytoplasm; Helicase; Hydrolase; Isopeptide bond; Methylation; KW Nucleotide-binding; Nucleus; Phosphoprotein; Proteomics identification; KW Reference proteome; RNA-binding; Ubl conjugation. FT CHAIN 1..938 FT /note="ATP-dependent RNA helicase DDX42" FT /id="PRO_0000280058" FT DOMAIN 284..459 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 487..632 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 1..114 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 182..203 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 737..938 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 738..833 FT /note="Necessary for interaction with TP53BP2" FT /evidence="ECO:0000269|PubMed:19377511" FT COILED 116..157 FT /evidence="ECO:0000255" FT MOTIF 253..281 FT /note="Q motif" FT MOTIF 407..410 FT /note="DEAD box" FT COMPBIAS 1..18 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 35..52 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 70..84 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 737..757 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 786..798 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 820..920 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 297..304 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT MOD_RES 5 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 12 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 96 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 104 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 109 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231" FT MOD_RES 111 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231" FT MOD_RES 185 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 754 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 899 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..119 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10727850, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|Ref.2" FT /id="VSP_023518" FT HELIX 71..76 FT /evidence="ECO:0007829|PDB:7EVN" FT HELIX 115..131 FT /evidence="ECO:0007829|PDB:7EVN" FT TURN 132..134 FT /evidence="ECO:0007829|PDB:7EVN" FT HELIX 149..152 FT /evidence="ECO:0007829|PDB:7EVN" FT HELIX 156..166 FT /evidence="ECO:0007829|PDB:7EVN" FT HELIX 222..225 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 229..238 FT /evidence="ECO:0007829|PDB:8DPE" FT STRAND 241..247 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 248..251 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 255..258 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 262..270 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 278..288 FT /evidence="ECO:0007829|PDB:8DPE" FT STRAND 293..296 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 303..316 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 319..322 FT /evidence="ECO:0007829|PDB:8DPE" FT STRAND 328..332 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 336..350 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 351..353 FT /evidence="ECO:0007829|PDB:8DPE" FT STRAND 357..360 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 366..375 FT /evidence="ECO:0007829|PDB:8DPE" FT STRAND 378..382 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 384..392 FT /evidence="ECO:0007829|PDB:8DPE" FT STRAND 403..406 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 409..414 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 418..427 FT /evidence="ECO:0007829|PDB:8DPE" FT STRAND 432..440 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 443..452 FT /evidence="ECO:0007829|PDB:8DPE" FT STRAND 457..461 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 462..464 FT /evidence="ECO:0007829|PDB:8DPE" FT STRAND 472..477 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 481..483 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 484..496 FT /evidence="ECO:0007829|PDB:8DPE" FT STRAND 499..507 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 508..520 FT /evidence="ECO:0007829|PDB:8DPE" FT STRAND 525..528 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 534..545 FT /evidence="ECO:0007829|PDB:8DPE" FT STRAND 548..555 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 556..558 FT /evidence="ECO:0007829|PDB:8DPE" FT STRAND 567..572 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 579..586 FT /evidence="ECO:0007829|PDB:8DPE" FT TURN 590..593 FT /evidence="ECO:0007829|PDB:8DPE" FT STRAND 597..602 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 604..606 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 607..619 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 626..632 FT /evidence="ECO:0007829|PDB:8DPE" FT HELIX 636..639 FT /evidence="ECO:0007829|PDB:8DPE" SQ SEQUENCE 938 AA; 102975 MW; D89A252E095D8913 CRC64; MNWNKGGPGT KRGFGFGGFA ISAGKKEEPK LPQQSHSAFG ATSSSSGFGK SAPPQLPSFY KIGSKRANFD EENAYFEDEE EDSSNVDLPY IPAENSPTRQ QFHSKPVDSD SDDDPLEAFM AEVEDQAARD MKRLEEKDKE RKNVKGIRDD IEEEDDQEAY FRYMAENPTA GVVQEEEEDN LEYDSDGNPI APTKKIIDPL PPIDHSEIDY PPFEKNFYNE HEEITNLTPQ QLIDLRHKLN LRVSGAAPPR PGSSFAHFGF DEQLMHQIRK SEYTQPTPIQ CQGVPVALSG RDMIGIAKTG SGKTAAFIWP MLIHIMDQKE LEPGDGPIAV IVCPTRELCQ QIHAECKRFG KAYNLRSVAV YGGGSMWEQA KALQEGAEIV VCTPGRLIDH VKKKATNLQR VSYLVFDEAD RMFDMGFEYQ VRSIASHVRP DRQTLLFSAT FRKKIEKLAR DILIDPIRVV QGDIGEANED VTQIVEILHS GPSKWNWLTR RLVEFTSSGS VLLFVTKKAN AEELANNLKQ EGHNLGLLHG DMDQSERNKV ISDFKKKDIP VLVATDVAAR GLDIPSIKTV INYDVARDID THTHRIGRTG RAGEKGVAYT LLTPKDSNFA GDLVRNLEGA NQHVSKELLD LAMQNAWFRK SRFKGGKGKK LNIGGGGLGY RERPGLGSEN MDRGNNNVMS NYEAYKPSTG AMGDRLTAMK AAFQSQYKSH FVAASLSNQK AGSSAAGASG WTSAGSLNSV PTNSAQQGHN SPDSPVTSAA KGIPGFGNTG NISGAPVTYP SAGAQGVNNT ASGNNSREGT GGSNGKRERY TENRGSSRHS HGETGNRHSD SPRHGDGGRH GDGYRHPESS SRHTDGHRHG ENRHGGSAGR HGENRGANDG RNGESRKEAF NRESKMEPKM EPKVDSSKMD KVDSKTDKTA DGFAVPEPPK RKKSRWDS //