DDX42_HUMAN
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 03-AUG-2022, entry version 170.
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).
CC -!- FUNCTION: ATP-dependent RNA helicase. Binds to partially double-
CC stranded RNAs (dsRNAs) in order to unwind RNA secondary structures.
CC Unwinding is promoted in the presence of single-strand binding
CC proteins. Mediates also RNA duplex formation thereby displacing the
CC single-strand RNA binding protein. ATP and ADP modulate its activity:
CC ATP binding and hydrolysis by DDX42 triggers RNA strand separation,
CC whereas the ADP-bound form of the protein triggers annealing of
CC complementary RNA strands. Involved in the survival of cells by
CC interacting with TP53BP2 and thereby counteracting the apoptosis-
CC stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm.
CC {ECO:0000269|PubMed:16397294, ECO:0000269|PubMed:19377511}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:16397294};
CC -!- SUBUNIT: Component of splicing factor SF3B complex which is composed of
CC at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6,
CC PHF5A/SF3B14B, and DDX42/SF3B125. Interacts (via the C-terminus) with
CC TP53BP2; the interaction is not inhibitied by TP53BP2 ubiquitination
CC and is independent of p53/TP53. {ECO:0000269|PubMed:12234937,
CC ECO:0000269|PubMed:19377511}.
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};
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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_203499.2. [Q86XP3-1]
DR RefSeq; XP_006721720.1; XM_006721657.1. [Q86XP3-1]
DR RefSeq; XP_016879600.1; XM_017024111.1. [Q86XP3-1]
DR AlphaFoldDB; Q86XP3; -.
DR SMR; Q86XP3; -.
DR BioGRID; 116454; 163.
DR CORUM; Q86XP3; -.
DR IntAct; Q86XP3; 48.
DR MINT; Q86XP3; -.
DR STRING; 9606.ENSP00000464050; -.
DR ChEMBL; CHEMBL4105782; -.
DR GlyGen; Q86XP3; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q86XP3; -.
DR MetOSite; Q86XP3; -.
DR PhosphoSitePlus; Q86XP3; -.
DR SwissPalm; Q86XP3; -.
DR BioMuta; DDX42; -.
DR DMDM; 74750541; -.
DR EPD; Q86XP3; -.
DR jPOST; Q86XP3; -.
DR MassIVE; Q86XP3; -.
DR MaxQB; Q86XP3; -.
DR PaxDb; Q86XP3; -.
DR PeptideAtlas; Q86XP3; -.
DR PRIDE; Q86XP3; -.
DR ProteomicsDB; 70312; -. [Q86XP3-1]
DR ProteomicsDB; 70313; -. [Q86XP3-2]
DR Antibodypedia; 18710; 105 antibodies from 20 providers.
DR DNASU; 11325; -.
DR Ensembl; ENST00000359353.9; ENSP00000352308.5; ENSG00000198231.14. [Q86XP3-2]
DR Ensembl; ENST00000389924.7; ENSP00000374574.2; ENSG00000198231.14. [Q86XP3-1]
DR Ensembl; ENST00000578681.5; ENSP00000464050.1; ENSG00000198231.14. [Q86XP3-1]
DR Ensembl; ENST00000583590.5; ENSP00000463561.1; ENSG00000198231.14. [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 CTD; 11325; -.
DR DisGeNET; 11325; -.
DR GeneCards; DDX42; -.
DR HGNC; HGNC:18676; DDX42.
DR HPA; ENSG00000198231; Low tissue specificity.
DR MIM; 613369; gene.
DR neXtProt; NX_Q86XP3; -.
DR OpenTargets; ENSG00000198231; -.
DR PharmGKB; PA134875761; -.
DR VEuPathDB; HostDB:ENSG00000198231; -.
DR eggNOG; KOG0339; Eukaryota.
DR GeneTree; ENSGT00940000156559; -.
DR InParanoid; Q86XP3; -.
DR OMA; FRSQYNS; -.
DR OrthoDB; 245118at2759; -.
DR PhylomeDB; Q86XP3; -.
DR TreeFam; TF300351; -.
DR PathwayCommons; Q86XP3; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR SignaLink; Q86XP3; -.
DR BioGRID-ORCS; 11325; 509 hits in 1097 CRISPR screens.
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 203 other tissues.
DR ExpressionAtlas; Q86XP3; baseline and differential.
DR Genevisible; Q86XP3; HS.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR GO; GO:0003724; F:RNA helicase activity; IDA:FlyBase.
DR GO; GO:0008104; P:protein localization; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; 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 Acetylation; Alternative splicing; ATP-binding; Coiled coil; Cytoplasm;
KW Helicase; Hydrolase; Isopeptide bond; Methylation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; 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 35..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..104
FT /note="Polar 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 771..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..938
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"
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
