GenomeNet

Database: UniProt
Entry: Q810A7
LinkDB: Q810A7
Original site: Q810A7 
ID   DDX42_MOUSE             Reviewed;         929 AA.
AC   Q810A7; Q3TAN3; Q3TE60; Q8BWZ7; Q9D8Q2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   16-OCT-2019, entry version 143.
DE   RecName: Full=ATP-dependent RNA helicase DDX42;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 42;
GN   Name=Ddx42;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Embryonic stem cell, Pancreas, Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [4]
RP   PROTEIN SEQUENCE OF 616-626, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-109, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-109; SER-111
RP   AND SER-185, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [11]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-12, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
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.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., 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).
CC   -!- FUNCTION: ATP-dependent RNA helicase. Binds to partially double-
CC       stranded RNAs (dsRNAs) in order to unwind RNA secondary
CC       structures. Unwinding is promoted in the presence of single-strand
CC       binding proteins. Mediates also RNA duplex formation thereby
CC       displacing the single-strand RNA binding protein. ATP and ADP
CC       modulate its activity: ATP binding and hydrolysis by DDX42
CC       triggers RNA strand separation, whereas the ADP-bound form of the
CC       protein triggers annealing of complementary RNA strands. Involved
CC       in the survival of cells by interacting with TP53BP2 and thereby
CC       counteracting the apoptosis-stimulating activity of TP53BP2.
CC       Relocalizes TP53BP2 to the cytoplasm (By similarity).
CC       {ECO:0000250}.
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: Component of splicing factor SF3B complex which is
CC       composed of at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4,
CC       SF3B5, SF3B6, PHF5A/SF3B14B, and DDX42/SF3B125. Interacts (via the
CC       C-terminus) with TP53BP2; the interaction is not inhibitied by
CC       TP53BP2 ubiquitination and is independent of p53/TP53 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus speckle
CC       {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q810A7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q810A7-2; Sequence=VSP_023519;
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX42
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH43036.4; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AK007805; BAB25270.3; -; mRNA.
DR   EMBL; AK049311; BAC33675.1; -; mRNA.
DR   EMBL; AK169816; BAE41388.1; -; mRNA.
DR   EMBL; AK171730; BAE42635.1; -; mRNA.
DR   EMBL; AL604045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC043036; AAH43036.4; ALT_INIT; mRNA.
DR   CCDS; CCDS48956.1; -. [Q810A7-1]
DR   RefSeq; NP_082350.3; NM_028074.4. [Q810A7-1]
DR   SMR; Q810A7; -.
DR   BioGrid; 215115; 2.
DR   IntAct; Q810A7; 2.
DR   MINT; Q810A7; -.
DR   STRING; 10090.ENSMUSP00000021046; -.
DR   iPTMnet; Q810A7; -.
DR   PhosphoSitePlus; Q810A7; -.
DR   EPD; Q810A7; -.
DR   jPOST; Q810A7; -.
DR   PaxDb; Q810A7; -.
DR   PeptideAtlas; Q810A7; -.
DR   PRIDE; Q810A7; -.
DR   Ensembl; ENSMUST00000021046; ENSMUSP00000021046; ENSMUSG00000020705. [Q810A7-1]
DR   GeneID; 72047; -.
DR   KEGG; mmu:72047; -.
DR   UCSC; uc007lyk.2; mouse. [Q810A7-1]
DR   CTD; 11325; -.
DR   MGI; MGI:1919297; Ddx42.
DR   eggNOG; KOG0334; Eukaryota.
DR   eggNOG; ENOG410XSQV; LUCA.
DR   GeneTree; ENSGT00940000156559; -.
DR   HOGENOM; HOG000268793; -.
DR   InParanoid; Q810A7; -.
DR   KO; K12835; -.
DR   OMA; FRSQYNS; -.
DR   OrthoDB; 245118at2759; -.
DR   PhylomeDB; Q810A7; -.
DR   TreeFam; TF300351; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR   ChiTaRS; Ddx42; mouse.
DR   PRO; PR:Q810A7; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000020705; Expressed in 269 organ(s), highest expression level in embryo.
DR   Genevisible; Q810A7; MM.
DR   GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
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;
KW   Complete proteome; Cytoplasm; Direct protein sequencing; Helicase;
KW   Hydrolase; Isopeptide bond; Methylation; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT   CHAIN         1    929       ATP-dependent RNA helicase DDX42.
FT                                /FTId=PRO_0000280059.
FT   DOMAIN      284    459       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      487    632       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     297    304       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION      739    828       Necessary for interaction with TP53BP2.
FT                                {ECO:0000250}.
FT   COILED      116    157       {ECO:0000255}.
FT   MOTIF       253    281       Q motif.
FT   MOTIF       407    410       DEAD box.
FT   COMPBIAS     43     46       Poly-Ser.
FT   COMPBIAS    175    178       Poly-Glu.
FT   COMPBIAS    654    659       Poly-Gly.
FT   COMPBIAS    675    678       Poly-Asn.
FT   COMPBIAS    784    878       Gly-rich.
FT   MOD_RES       5      5       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q86XP3}.
FT   MOD_RES      12     12       Omega-N-methylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES      58     58       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q86XP3}.
FT   MOD_RES      96     96       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q86XP3}.
FT   MOD_RES     104    104       Phosphoserine.
FT                                {ECO:0000244|PubMed:17622165,
FT                                ECO:0000244|PubMed:19144319,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     109    109       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:19144319,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     111    111       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     185    185       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CROSSLNK    894    894       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q86XP3}.
FT   VAR_SEQ       1    119       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_023519.
FT   CONFLICT    503    503       L -> M (in Ref. 1; BAB25270).
FT                                {ECO:0000305}.
FT   CONFLICT    537    537       R -> G (in Ref. 1; BAE42635).
FT                                {ECO:0000305}.
FT   CONFLICT    859    859       H -> Y (in Ref. 1; BAC33675).
FT                                {ECO:0000305}.
SQ   SEQUENCE   929 AA;  101965 MW;  0E8F3D30D07BDFCF CRC64;
     MNWNKGGPGT KRGFGFGGFA ISAGKKEEAK LPQQSHSAFG AASSSSGFGK SAPPQLPSFY
     KIGSKRANFD EENAYFEDEE EDSSNVDLPY IPAENSPTRQ QFHSKPADSD SDDDPLEAFM
     AEVEDQAARD MKRLEEKDKE RKNVKGIRDD IEEEDDQEAY FRYMAENPTA GVVQEEEEDN
     LEYDSDGNPI APSKKIIDPL 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 AEELASNLKQ EGHNLGLLHG DMDQSERNKV
     ISDFKKKDIP VLVATDVAAR GLDIPSIKTV INYDVARDID THTHRIGRTG RAGEKGVAYT
     LLTPKDSNFA GDLVRNLEGA NQHVSKELLD LAMQNAWFRK SRFKGGKGKK LNIGGGGLGY
     RERPGLGSEN SDRGNNNNVM SNYEAYKPST GAMGDRLTAM KAAFQSQYKS HFVAASLSNQ
     KAGTSSAGAS GWTSAGSLNS VPTNSAQQGH NSPDNPMTSS TKNIPGFNNS GNISSAPVTY
     PSIGAQGVNN TASGNNSREG IGGGNGKRER YTENRGGSRH SHGDGGNRHG DGGRHGDGYR
     YPESGSRHTD GHRHGETRHG GSAGRHGESR GANDGRNGES RKEGFNRENK MDPKVDSSRM
     DKVDSKTDKT PDGFAVPEPP KRKKSRWDS
//
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