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Database: UniProt
Entry: O70133
LinkDB: O70133
Original site: O70133 
ID   DHX9_MOUSE              Reviewed;        1380 AA.
AC   O70133; O35931; O54703; Q5FWY1; Q6R5F7; Q9CSA2;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   16-OCT-2019, entry version 177.
DE   RecName: Full=ATP-dependent RNA helicase A {ECO:0000250|UniProtKB:Q08211};
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:Q08211};
DE   AltName: Full=DEAH box protein 9 {ECO:0000303|Ref.5};
DE            Short=mHEL-5 {ECO:0000303|Ref.5};
DE   AltName: Full=Nuclear DNA helicase II {ECO:0000250|UniProtKB:Q08211};
DE            Short=NDH II {ECO:0000250|UniProtKB:Q08211};
DE   AltName: Full=RNA helicase A {ECO:0000303|PubMed:9480750};
DE            Short=RHA {ECO:0000303|PubMed:9480750};
GN   Name=Dhx9 {ECO:0000312|MGI:MGI:108177};
GN   Synonyms=Ddx9 {ECO:0000250|UniProtKB:Q08211};
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 [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP   [GENOMIC DNA] OF 1-161.
RC   STRAIN=129/Sv;
RX   PubMed=9480750; DOI=10.1006/geno.1997.5139;
RA   Lee C.-G., Eki T., Okumura K., da Costa Soares V., Hurwitz J.;
RT   "Molecular analysis of the cDNA and genomic DNA encoding mouse RNA
RT   helicase A.";
RL   Genomics 47:365-371(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-756 (ISOFORM 3).
RC   STRAIN=C57BL/6NCr;
RX   PubMed=14691545; DOI=10.1371/journal.pbio.0000074;
RA   Sharov A.A., Piao Y., Matoba R., Dudekula D.B., Qian Y., VanBuren V.,
RA   Falco G., Martin P.R., Stagg C.A., Bassey U.C., Wang Y., Carter M.G.,
RA   Hamatani T., Aiba K., Akutsu H., Sharova L., Tanaka T.S., Kimber W.L.,
RA   Yoshikawa T., Jaradat S.A., Pantano S., Nagaraja R., Boheler K.R.,
RA   Taub D., Hodes R.J., Longo D.L., Schlessinger D., Keller J., Klotz E.,
RA   Kelsoe G., Umezawa A., Vescovi A.L., Rossant J., Kunath T.,
RA   Hogan B.L.M., Curci A., D'Urso M., Kelso J., Hide W., Ko M.S.H.;
RT   "Transcriptome analysis of mouse stem cells and early embryos.";
RL   PLoS Biol. 1:410-419(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-756 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-264 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
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   [5]
RP   NUCLEOTIDE SEQUENCE OF 386-919 (ISOFORMS 1/2/3).
RC   STRAIN=C57BL/6J;
RA   Kisielow P., Miazek A.;
RT   "mHEL-5.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10413677;
RA   Zhang S., Herrmann C., Grosse F.;
RT   "Nucleolar localization of murine nuclear DNA helicase II (RNA
RT   helicase A).";
RL   J. Cell Sci. 112:2693-2703(1999).
RN   [7]
RP   INTERACTION WITH SP7, AND SUBCELLULAR LOCATION.
RX   PubMed=17303075; DOI=10.1016/j.bbrc.2007.01.150;
RA   Amorim B.R., Okamura H., Yoshida K., Qiu L., Morimoto H., Haneji T.;
RT   "The transcriptional factor Osterix directly interacts with RNA
RT   helicase A.";
RL   Biochem. Biophys. Res. Commun. 355:347-351(2007).
RN   [8]
RP   INTERACTION WITH ZIC2.
RX   PubMed=17251188; DOI=10.1074/jbc.m610821200;
RA   Ishiguro A., Ideta M., Mikoshiba K., Chen D.J., Aruga J.;
RT   "ZIC2-dependent transcriptional regulation is mediated by DNA-
RT   dependent protein kinase, poly(ADP-ribose) polymerase, and RNA
RT   helicase A.";
RL   J. Biol. Chem. 282:9983-9995(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 2), AND
RP   IDENTIFICATION 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 2), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH EIF2AK2, AND
RP   PHOSPHORYLATION.
RX   PubMed=19229320; DOI=10.1371/journal.ppat.1000311;
RA   Sadler A.J., Latchoumanin O., Hawkes D., Mak J., Williams B.R.;
RT   "An antiviral response directed by PKR phosphorylation of the RNA
RT   helicase A.";
RL   PLoS Pathog. 5:E1000311-E1000311(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, PHOSPHORYLATION
RP   [LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 2), AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
RC   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   [13]
RP   FUNCTION IN CIRCADIAN RHYTHMS, AND IDENTIFICATION IN A LARGE PER
RP   COMPLEX.
RX   PubMed=22767893; DOI=10.1126/science.1221592;
RA   Padmanabhan K., Robles M.S., Westerling T., Weitz C.J.;
RT   "Feedback regulation of transcriptional termination by the mammalian
RT   circadian clock PERIOD complex.";
RL   Science 337:599-602(2012).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA   Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [15]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1167; ARG-1312; ARG-1323;
RP   ARG-1339; ARG-1346; ARG-1353; ARG-1361 AND ARG-1372, AND
RP   IDENTIFICATION BY 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).
RN   [16]
RP   FUNCTION, INTERACTION WITH ADAR, AND ALU RNA-BINDING.
RX   PubMed=28355180; DOI=10.1038/nature21715;
RA   Aktas T., Avsar Ilik I., Maticzka D., Bhardwaj V.,
RA   Pessoa Rodrigues C., Mittler G., Manke T., Backofen R., Akhtar A.;
RT   "DHX9 suppresses RNA processing defects originating from the Alu
RT   invasion of the human genome.";
RL   Nature 544:115-119(2017).
RN   [17]
RP   FUNCTION.
RX   PubMed=28636595; DOI=10.1038/nature22967;
RA   Zhu S., Ding S., Wang P., Wei Z., Pan W., Palm N.W., Yang Y., Yu H.,
RA   Li H.B., Wang G., Lei X., de Zoete M.R., Zhao J., Zheng Y., Chen H.,
RA   Zhao Y., Jurado K.A., Feng N., Shan L., Kluger Y., Lu J., Abraham C.,
RA   Fikrig E., Greenberg H.B., Flavell R.A.;
RT   "Nlrp9b inflammasome restricts rotavirus infection in intestinal
RT   epithelial cells.";
RL   Nature 546:667-670(2017).
RN   [18]
RP   STRUCTURE BY NMR OF 4-262.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of double-stranded RNA-binding motifs from
RT   hypothetical protein BAB28848.";
RL   Submitted (NOV-2004) to the PDB data bank.
RN   [19]
RP   INTERACTION WITH ZIC2.
RX   PubMed=18068128; DOI=10.1016/j.febslet.2007.11.080;
RA   Ishiguro A., Aruga J.;
RT   "Functional role of Zic2 phosphorylation in transcriptional
RT   regulation.";
RL   FEBS Lett. 582:154-158(2008).
CC   -!- FUNCTION: Multifunctional ATP-dependent nucleic acid helicase that
CC       unwinds DNA and RNA in a 3' to 5' direction and that plays
CC       important roles in many processes, such as DNA replication,
CC       transcriptional activation, post-transcriptional RNA regulation,
CC       mRNA translation and RNA-mediated gene silencing. Requires a 3'-
CC       single-stranded tail as entry site for acid nuclei unwinding
CC       activities as well as the binding and hydrolyzing of any of the
CC       four ribo- or deoxyribo-nucleotide triphosphates (NTPs). Unwinds
CC       numerous nucleic acid substrates such as double-stranded (ds) DNA
CC       and RNA, DNA:RNA hybrids, DNA and RNA forks composed of either
CC       partially complementary DNA duplexes or DNA:RNA hybrids,
CC       respectively, and also DNA and RNA displacement loops (D- and R-
CC       loops), triplex-helical DNA (H-DNA) structure and DNA- and RNA-
CC       based G-quadruplexes. Binds dsDNA, single-stranded DNA (ssDNA),
CC       dsRNA, ssRNA and poly(A)-containing RNA. Binds also to circular
CC       dsDNA or dsRNA of either linear and/or circular forms and
CC       stimulates the relaxation of supercoiled DNAs catalyzed by
CC       topoisomerase TOP2A. Plays a role in DNA replication at origins of
CC       replication and cell cycle progression. Plays a role as a
CC       transcriptional coactivator acting as a bridging factor between
CC       polymerase II holoenzyme and transcription factors or cofactors,
CC       such as BRCA1, CREBBP, RELA and SMN1. Binds to the CDKN2A
CC       promoter. Plays several roles in post-transcriptional regulation
CC       of gene expression. In cooperation with NUP98, promotes pre-mRNA
CC       alternative splicing activities of a subset of genes (By
CC       similarity). As component of a large PER complex, is involved in
CC       the negative regulation of 3' transcriptional termination of
CC       circadian target genes such as PER1 and NR1D1 and the control of
CC       the circadian rhythms (PubMed:22767893). Acts also as a nuclear
CC       resolvase that is able to bind and neutralize harmful massive
CC       secondary double-stranded RNA structures formed by inverted-repeat
CC       Alu retrotransposon elements that are inserted and transcribed as
CC       parts of genes during the process of gene transposition
CC       (PubMed:28355180). Involved in the positive regulation of nuclear
CC       export of constitutive transport element (CTE)-containing
CC       unspliced mRNA. Component of the coding region determinant (CRD)-
CC       mediated complex that promotes cytoplasmic MYC mRNA stability.
CC       Plays a role in mRNA translation. Positively regulates translation
CC       of selected mRNAs through its binding to post-transcriptional
CC       control element (PCE) in the 5'-untranslated region (UTR).
CC       Involved with LARP6 in the translation stimulation of type I
CC       collagen mRNAs for CO1A1 and CO1A2 through binding of a specific
CC       stem-loop structure in their 5'-UTRs. Stimulates LIN28A-dependent
CC       mRNA translation probably by facilitating ribonucleoprotein
CC       remodeling during the process of translation. Plays also a role as
CC       a small interfering (siRNA)-loading factor involved in the RNA-
CC       induced silencing complex (RISC) loading complex (RLC) assembly,
CC       and hence functions in the RISC-mediated gene silencing process.
CC       Binds preferentially to short double-stranded RNA, such as those
CC       produced during rotavirus intestinal infection (PubMed:28636595).
CC       This interaction may mediate NLRP9 inflammasome activation and
CC       trigger inflammatory response, including IL18 release and
CC       pyroptosis (PubMed:28636595). Finally, mediates the attachment of
CC       heterogeneous nuclear ribonucleoproteins (hnRNPs) to actin
CC       filaments in the nucleus (By similarity).
CC       {ECO:0000250|UniProtKB:Q08211, ECO:0000269|PubMed:22767893,
CC       ECO:0000269|PubMed:28355180, ECO:0000269|PubMed:28636595}.
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:0000250|UniProtKB:Q08211};
CC   -!- SUBUNIT: Component of the coding region determinant (CRD)-mediated
CC       complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1.
CC       Identified in a mRNP complex, at least composed of DHX9, DDX3X,
CC       ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2,
CC       SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule
CC       complex containing untranslated mRNAs (By similarity). The large
CC       PER complex involved in the repression of transcriptional
CC       termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1
CC       and POLR2A (active) (PubMed:22767893). Associates (via DRBM
CC       domains) with the RISC complex; this association occurs in a small
CC       interfering (siRNA)-dependent manner. Associates with the SMN
CC       complex; this association induces recruitment of DHX9 to the RNA
CC       polymerase II. Associates with polysomes in a LIN28A-dependent
CC       manner. Interacts (via C-terminus) with ACTB; this interaction is
CC       direct and mediates the attachment to nuclear ribonucleoprotein
CC       complexes (By similarity). Interacts with ADAR isoform 1; this
CC       interaction occurs in a RNA-independent manner (PubMed:28355180).
CC       Interacts (via DRBM domains) with AGO2 (via middle region); this
CC       interaction promotes active RISC assembly by promoting the
CC       association of siRNA with AGO2. Interacts (via NTD domain) with
CC       AKAP8L (via N-terminus). Interacts with BRCA1 (via C-terminus);
CC       this interaction is direct and links BRCA1 to the RNA polymerase
CC       II holoenzyme. Interacts (via N-terminus) with CREBBP; this
CC       interaction mediates association with RNA polymerase II holoenzyme
CC       and stimulates CREB-dependent transcriptional activation (By
CC       similarity). Interacts (via N-terminus) with EIF2AK2/PKR; this
CC       interaction is dependent upon the activation of the kinase
CC       (PubMed:19229320). Interacts (via DRBM domains) with DICER1.
CC       Interacts with H2AFX; this interaction is direct, requires
CC       phosphorylation of histone H2AFX on 'Ser-140' by PRKDC and
CC       promotes binding of DHX9 to transcriptionally stalled sites on
CC       chromosomal DNA in response to genotoxic stress. Interacts with
CC       HNRNPC; this interaction is direct, enhanced probably by their
CC       concomitant binding to RNA and mediates the attachment to actin
CC       filaments. Interacts (via NTD domain) with PRMT1. Interacts with
CC       IGF2BP1. Interacts with IGF2BP2, IGF2BP3. Interacts (via DRBM
CC       domains) with ILF3; this interaction occurs in a RNA-independent
CC       manner. Interacts with Importin alpha/Importin beta receptor.
CC       Interacts with LARP6 (via C-terminus); this interaction occurs in
CC       a mRNA-independent manner. Interacts (via N- and C-terminus) with
CC       LIN28A (via C-terminus); this interaction occurs in a RNA-
CC       independent manner. Interacts with LMX1B. Interacts (via helicase
CC       C-terminal domain, HA2 and OB-fold regions) with MAVS (via CARD
CC       domain); this interaction occurs in both resting and double-
CC       stranded RNA poly(I:C)-induced cells. Interacts with MBD2; this
CC       interaction stimulates transcriptional activation in a CREB-
CC       dependent manner. Interacts (via H2A and OB-fold regions) with
CC       MYD88 (via TIR domain); this interaction is direct. Interacts with
CC       NLRP9 upon rotavirus infection; this interaction may trigger NLRP9
CC       inflammasome activation and inflammatory response. Interacts (via
CC       DRBM, OB-fold and RGG regions) with NUP98 (via N-terminus); this
CC       interaction occurs in a RNA-dependent manner and stimulates DHX9-
CC       mediated ATPase activity and regulates transcription and splicing
CC       of a subset of genes. Interacts (via N-terminus) with NXF1 (via N-
CC       terminus); this interaction is direct and negatively regulates
CC       NXF1-mediated nuclear export of constitutive transport element
CC       (CTE)-containing cellular mRNAs. Interacts with RELA; this
CC       interaction is direct and activates NF-kappa-B-mediated
CC       transcription. Interacts (via MTAD region) with RNA polymerase II
CC       holoenzyme; this interaction stimulates transcription activation
CC       in a CREB-dependent manner. Interacts (via RGG region) with SMN1;
CC       this interaction links SMN1 to the RNA polymerase II holoenzyme
CC       (By similarity). Interacts with SP7 (PubMed:17303075). Interacts
CC       (via DRBM domains) with TARBP2 (via DRBM first and second
CC       domains); this interaction occurs in a small interfering (siRNA)-
CC       dependent manner. Interacts with TOP2A; this interaction occurs in
CC       a E2 enzyme UBE2I- and RNA-dependent manner, negatively regulates
CC       DHX9-mediated double-stranded DNA and RNA duplex helicase activity
CC       and stimulates TOP2A-mediated supercoiled DNA relaxation activity.
CC       Interacts (via DRBM domains and C-terminus) with WRN (via 3'-5'
CC       exonuclease domain); this interaction inhibits the DNA-dependent
CC       NTPase and DNA helicase activities of DHX9 and stimulates the 3'-
CC       5' exonuclease activity of WRN. Interacts with XRCC5; this
CC       interaction occurs in a RNA-dependent manner (By similarity).
CC       Interacts with ZIC2 (via C2H2-type domain 3) (PubMed:17251188).
CC       Interacts with MCM3AP (By similarity).
CC       {ECO:0000250|UniProtKB:Q08211, ECO:0000269|PubMed:17251188,
CC       ECO:0000269|PubMed:17303075, ECO:0000269|PubMed:19229320,
CC       ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:28355180}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17303075}.
CC       Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q08211}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:10413677}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q08211}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:Q08211}. Note=Nucleoplasmic shuttling
CC       protein. Its nuclear import involves the nucleocytoplasmic
CC       transport receptor Importin alpha/Importin beta receptor pathway
CC       in a Ran-dependent manner. In interphase, localizes in nuclear
CC       stress granules and at perichromatin fibrils and in cytoplasmic
CC       ribonucleoprotein granules. Colocalizes with WRN and H2AFX at
CC       centrosomes in a microtubule-dependent manner following DNA
CC       damaging agent treatment. Excluded from the mitotic nucleus as
CC       early as prophase and re-entered the nucleus at telophase.
CC       Recruited in diffuse and discrete intranuclear foci (GLFG-body) in
CC       a NUP98-dependent manner (By similarity). Colocalizes with SP7 in
CC       the nucleus (PubMed:17303075). Colocalizes with ACTB at nuclear
CC       actin filaments inside the nucleus or at the nuclear pore.
CC       Colocalizes with HNRNPC at nuclear ribonucleoprotein complex
CC       proteins in the nucleus. Localized in cytoplasmic mRNP granules
CC       containing untranslated mRNAs (By similarity).
CC       {ECO:0000250|UniProtKB:Q08211, ECO:0000269|PubMed:17303075}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O70133-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O70133-2; Sequence=VSP_014779;
CC         Note=Contains a phosphoserine at position 137.
CC         {ECO:0000244|PubMed:17242355, ECO:0000244|PubMed:18630941,
CC         ECO:0000244|PubMed:21183079};
CC       Name=3;
CC         IsoId=O70133-3; Sequence=VSP_014778;
CC   -!- DOMAIN: DRBM domains cooperate for the binding to nucleic acid but
CC       not for unwinding helicase activity. The helicase-associated
CC       domain-2 (HA2) region is essential for the duplex RNA unwinding
CC       helicase activity. The minimal transactivation region (MTAD)
CC       mediates interaction with the RNA polymerase II holoenzyme and
CC       stimulates transcriptional activation in a CREB-dependent manner.
CC       The oligonucleotide- or oligosaccharide-binding (OB-fold) and the
CC       repeated arginine and glycine-glycine (RGG) regions are
CC       dispensable for both RNA-binding and unwinding helicase
CC       activities. The RGG region contains both nuclear localization
CC       signal (NLS) and nuclear export signal (NES) and is necessary and
CC       sufficient for nucleocytoplasmic shuttling in a RNA-independent
CC       manner. {ECO:0000250|UniProtKB:Q08211}.
CC   -!- PTM: Methylated. PRMT1-mediated methylation of undefined Arg
CC       residues in the nuclear transport domain (NTD) is required for
CC       nuclear import of DHX9. {ECO:0000250|UniProtKB:Q08211}.
CC   -!- PTM: Phosphorylated by PRKDC; phosphorylation occurs in a RNA-
CC       dependent manner. Phosphorylated by EIF2AK2/PKR; this
CC       phosphorylation reduces its association with double-stranded RNA.
CC       {ECO:0000250|UniProtKB:Q08211}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH89159.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAR87796.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
DR   EMBL; U91922; AAC05725.1; -; mRNA.
DR   EMBL; AF023530; AAC05301.1; -; Genomic_DNA.
DR   EMBL; AY512925; AAR87796.1; ALT_SEQ; mRNA.
DR   EMBL; BC089159; AAH89159.1; ALT_SEQ; mRNA.
DR   EMBL; AK013423; BAB28848.1; -; mRNA.
DR   EMBL; U92080; AAB72087.1; -; mRNA.
DR   RefSeq; NP_031868.2; NM_007842.2.
DR   PDB; 1UIL; NMR; -; A=163-262.
DR   PDB; 1WHQ; NMR; -; A=4-89.
DR   PDB; 2RS6; NMR; -; A=4-89.
DR   PDB; 2RS7; NMR; -; A=163-262.
DR   PDBsum; 1UIL; -.
DR   PDBsum; 1WHQ; -.
DR   PDBsum; 2RS6; -.
DR   PDBsum; 2RS7; -.
DR   SMR; O70133; -.
DR   BioGrid; 199088; 11.
DR   ComplexPortal; CPX-1089; CRD-mediated mRNA stability complex.
DR   IntAct; O70133; 12.
DR   MINT; O70133; -.
DR   STRING; 10090.ENSMUSP00000038135; -.
DR   iPTMnet; O70133; -.
DR   PhosphoSitePlus; O70133; -.
DR   SwissPalm; O70133; -.
DR   EPD; O70133; -.
DR   jPOST; O70133; -.
DR   MaxQB; O70133; -.
DR   PaxDb; O70133; -.
DR   PeptideAtlas; O70133; -.
DR   PRIDE; O70133; -.
DR   GeneID; 13211; -.
DR   KEGG; mmu:13211; -.
DR   CTD; 1660; -.
DR   MGI; MGI:108177; Dhx9.
DR   eggNOG; KOG0920; Eukaryota.
DR   eggNOG; COG1643; LUCA.
DR   HOGENOM; HOG000247063; -.
DR   InParanoid; O70133; -.
DR   KO; K13184; -.
DR   OrthoDB; 278674at2759; -.
DR   PhylomeDB; O70133; -.
DR   Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1.
DR   Reactome; R-MMU-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   ChiTaRS; Dhx9; mouse.
DR   EvolutionaryTrace; O70133; -.
DR   PRO; PR:O70133; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISS:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR   GO; GO:0097165; C:nuclear stress granule; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005726; C:perichromatin fibrils; ISS:UniProtKB.
DR   GO; GO:0042788; C:polysomal ribosome; ISS:UniProtKB.
DR   GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0016442; C:RISC complex; ISS:UniProtKB.
DR   GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0033679; F:3'-5' DNA/RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0034458; F:3'-5' RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISO:MGI.
DR   GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
DR   GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0003688; F:DNA replication origin binding; ISS:UniProtKB.
DR   GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR   GO; GO:0061676; F:importin-alpha family protein binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; ISS:UniProtKB.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; ISS:UniProtKB.
DR   GO; GO:1905538; F:polysome binding; ISS:UniProtKB.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR   GO; GO:0001069; F:regulatory region RNA binding; IDA:UniProtKB.
DR   GO; GO:1905172; F:RISC complex binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
DR   GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
DR   GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
DR   GO; GO:1990518; F:single-stranded 3'-5' DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR   GO; GO:0035197; F:siRNA binding; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR   GO; GO:0045142; F:triplex DNA binding; ISS:UniProtKB.
DR   GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0034622; P:cellular protein-containing complex assembly; ISO:MGI.
DR   GO; GO:0071360; P:cellular response to exogenous dsRNA; ISS:UniProtKB.
DR   GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR   GO; GO:0007623; P:circadian rhythm; IMP:MGI.
DR   GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISO:MGI.
DR   GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR   GO; GO:0039695; P:DNA-templated viral transcription; ISO:MGI.
DR   GO; GO:0044806; P:G-quadruplex DNA unwinding; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISS:UniProtKB.
DR   GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR   GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR   GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; ISS:UniProtKB.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR   GO; GO:2000637; P:positive regulation of gene silencing by miRNA; ISS:UniProtKB.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IMP:UniProtKB.
DR   GO; GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB.
DR   GO; GO:1902741; P:positive regulation of interferon-alpha secretion; ISS:UniProtKB.
DR   GO; GO:0035549; P:positive regulation of interferon-beta secretion; ISS:UniProtKB.
DR   GO; GO:0032741; P:positive regulation of interleukin-18 production; IMP:UniProtKB.
DR   GO; GO:2000778; P:positive regulation of interleukin-6 secretion; ISS:UniProtKB.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:1905698; P:positive regulation of polysome binding; ISS:UniProtKB.
DR   GO; GO:0060760; P:positive regulation of response to cytokine stimulus; ISS:UniProtKB.
DR   GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; ISS:UniProtKB.
DR   GO; GO:0050434; P:positive regulation of viral transcription; ISO:MGI.
DR   GO; GO:1904973; P:positive regulation of viral translation; ISO:MGI.
DR   GO; GO:1903608; P:protein localization to cytoplasmic stress granule; ISO:MGI.
DR   GO; GO:0070269; P:pyroptosis; IMP:UniProtKB.
DR   GO; GO:2000765; P:regulation of cytoplasmic translation; ISS:UniProtKB.
DR   GO; GO:0050691; P:regulation of defense response to virus by host; IMP:UniProtKB.
DR   GO; GO:0050684; P:regulation of mRNA processing; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0010501; P:RNA secondary structure unwinding; ISS:UniProtKB.
DR   GO; GO:0070922; P:small RNA loading onto RISC; ISS:UniProtKB.
DR   GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; ISS:UniProtKB.
DR   CDD; cd00048; DSRM; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00035; dsrm; 2.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00358; DSRM; 2.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS50137; DS_RBD; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative splicing;
KW   ATP-binding; Biological rhythms; Complete proteome; Cytoplasm;
KW   Cytoskeleton; DNA-binding; Helicase; Hydrolase; Immunity;
KW   Inflammatory response; Innate immunity; Isopeptide bond;
KW   Metal-binding; Methylation; mRNA processing; mRNA splicing;
KW   mRNA transport; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
KW   Transcription; Transcription regulation; Transcription termination;
KW   Translation regulation; Transport; Ubl conjugation.
FT   CHAIN         1   1380       ATP-dependent RNA helicase A.
FT                                /FTId=PRO_0000055158.
FT   DOMAIN        3     71       DRBM 1. {ECO:0000250|UniProtKB:Q08211,
FT                                ECO:0000255|PROSITE-ProRule:PRU00266}.
FT   DOMAIN      182    254       DRBM 2. {ECO:0000250|UniProtKB:Q08211,
FT                                ECO:0000255|PROSITE-ProRule:PRU00266}.
FT   DOMAIN      400    566       Helicase ATP-binding.
FT                                {ECO:0000250|UniProtKB:Q08211,
FT                                ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      638    811       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     413    421       ATP. {ECO:0000250|UniProtKB:Q08211,
FT                                ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   REGION        1    252       Interaction with CREBBP.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION        5      9       siRNA-binding.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION       53     55       siRNA-binding.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      184    188       siRNA-binding.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      232    327       Interaction with BRCA1.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      236    238       siRNA-binding.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      257    666       Necessary for interaction with RNA
FT                                polymerase II holoenzyme.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      315    954       Necessary for interaction with H2AFX.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      333    382       MTAD. {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      400    811       Core helicase.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      833    921       HA2. {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      960   1076       OB-fold. {ECO:0000250|UniProtKB:Q08211}.
FT   REGION     1151   1366       NTD region.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION     1152   1380       RGG. {ECO:0000250|UniProtKB:Q08211}.
FT   MOTIF       513    516       DEAH box.
FT   MOTIF       588    597       Nuclear localization signal (NLS1).
FT                                {ECO:0000255}.
FT   MOTIF      1156   1174       Nuclear localization signal (NLS2).
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   COMPBIAS   1171   1380       Arg/Gly/Ser/Tyr-rich.
FT   METAL       420    420       Manganese.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   METAL       514    514       Manganese.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES     127    127       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES     136    136       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     148    148       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     148    148       N6-methyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES     193    193       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES     201    201       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES     323    323       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES     451    451       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES     508    508       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES    1026   1026       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES    1167   1167       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    1176   1176       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES    1312   1312       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    1323   1323       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    1339   1339       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    1346   1346       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    1353   1353       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    1361   1361       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    1372   1372       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   CROSSLNK    699    699       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   VAR_SEQ       1    216       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14691545}.
FT                                /FTId=VSP_014778.
FT   VAR_SEQ     123    123       E -> EA (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_014779.
FT   CONFLICT     46     46       A -> R (in Ref. 1; AAC05725).
FT                                {ECO:0000305}.
FT   CONFLICT    136    136       S -> A (in Ref. 1; AAC05725/AAC05301).
FT                                {ECO:0000305}.
FT   CONFLICT    187    187       L -> V (in Ref. 2). {ECO:0000305}.
FT   CONFLICT    189    189       Q -> H (in Ref. 1; AAC05725).
FT                                {ECO:0000305}.
FT   CONFLICT    211    211       R -> G (in Ref. 4; BAB28848).
FT                                {ECO:0000305}.
FT   CONFLICT    235    235       S -> C (in Ref. 1; AAC05725).
FT                                {ECO:0000305}.
FT   CONFLICT    257    257       V -> C (in Ref. 1; AAC05725).
FT                                {ECO:0000305}.
FT   CONFLICT    281    281       S -> P (in Ref. 1; AAC05725).
FT                                {ECO:0000305}.
FT   CONFLICT    674    674       N -> M (in Ref. 5; AAB72087).
FT                                {ECO:0000305}.
FT   CONFLICT    748    748       T -> I (in Ref. 5; AAB72087).
FT                                {ECO:0000305}.
FT   CONFLICT    831    831       I -> V (in Ref. 5; AAB72087).
FT                                {ECO:0000305}.
FT   HELIX         5     14       {ECO:0000244|PDB:1WHQ}.
FT   STRAND       20     27       {ECO:0000244|PDB:1WHQ}.
FT   STRAND       29     39       {ECO:0000244|PDB:1WHQ}.
FT   STRAND       47     53       {ECO:0000244|PDB:1WHQ}.
FT   HELIX        54     72       {ECO:0000244|PDB:1WHQ}.
FT   TURN         77     79       {ECO:0000244|PDB:1WHQ}.
FT   HELIX       172    175       {ECO:0000244|PDB:1UIL}.
FT   HELIX       180    193       {ECO:0000244|PDB:1UIL}.
FT   STRAND      201    206       {ECO:0000244|PDB:1UIL}.
FT   STRAND      212    221       {ECO:0000244|PDB:1UIL}.
FT   TURN        222    225       {ECO:0000244|PDB:1UIL}.
FT   STRAND      226    231       {ECO:0000244|PDB:1UIL}.
FT   HELIX       237    255       {ECO:0000244|PDB:1UIL}.
SQ   SEQUENCE   1380 AA;  149475 MW;  005D641CD9A4F0C9 CRC64;
     MGDIKNFLYA WCGKRKMTPA YEIRAVGNKN RQKFMCEVRV EGFNYAGMGN STNKKDAQSN
     AARDFVNYLV RINEVKSEEV PAVGIVPPPP ILSDTSDSTA SAAEGLPAPM GGPLPPHLAL
     KAEENNSGVE SSGYGSPGPT WDRGANLKDY YSRKEEQEVQ ATLESEEVDL NAGLHGNWTL
     ENAKARLNQY FQKEKIQGEY KYTQVGPDHN RSFIAEMTIY IKQLGRRIFA REHGSNKKLA
     AQSCALSLVR QLYHLGVIEA YSGLTKKKEG ERVEPYKVFL SPDLELQLQN VVQELDLEIV
     PPPVDPSMPV ILNIGKLAHF EPSQRQNAVG VVPWSPPQSN WNPWTSSNID EGPLAYASTE
     QISMDLKNEL TYQMEQDHNL QSVLQERELL PVKKFEAEIL EAISSNSVVI IRGATGCGKT
     TQVPQYILDD FIQNDRAAEC NIVVTQPRRI SAVAVAERVA YERGEEPGKS CGYSVRFESI
     LPRPHASIMF CTVGVLLRKL EAGIRGISHV IVDEIHERDI NTDFLLVVLR DVVLAYPEVR
     IVLMSATIDT TMFCEYFFNC PIIEVYGRTF PVQEYFLEDC IQMTQFIPPP KDKKKKDKED
     DGGEDDDANC NLICGDEYGP ETKLSMSQLN EKETPFELIE ALLKYIETLN VPGAVLVFLP
     GWNLIYTMQK HLENNSHFGS HRYQILPLHS QIPREEQRKV FDPVPDGVTK VILSTNIAET
     SITINDVVYV IDSCKQKVKL FTAHNNMTNY ATVWASKTNL EQRKGRAGRV RPGFCFHLCS
     RARFDRLETH MTPEMFRTPL HEIALSIKLL RLGGIGQFLA KAIEPPPLDA IIEAEHTLRE
     LDALDANDEL TPLGRILAKL PIEPRFGKMM IMGCIFYVGD AVCTISAATC FPEPFISEGK
     RLGYIHRNFA GNRFSDHVAL LSVFQAWDDA RMSGEEAEIR FCEQKRLNMA TLRMTWEAKV
     QLKEILINSG FPEDCLLTQV FTNTGPDNNL DVVISLLAFG VYPNVCYHKE KRKILTTEGR
     NALIHKSSVN CPFSSQDMKY PSPFFVFGEK IRTRAISAKG MTLVTPLQLL LFASKKVQSD
     GQIVFIDDWI RLQISHEAAA CITIRAAMEA LVVEVSKQPN IISQLDPVNE HMLNTIRQIS
     RPSAAGINLM IGSVRYGDGP RPPKMARYDN GSGYRRGYGG GGYGGGGYGG GYGSGGFGGG
     FGSGGGFGGG FNSGGGGFGS GGGGFGSGGG GFGGGGGGFS GGGGGGFGGG RGGGGGGFGG
     SGGFGNGGGG YGVGGGGYGG GGGGGYGGGS GGYGGGGYGG GEGYSISPNS YRGNYGGGGG
     GYRGGSQGGY RNNFGGDYRG SSGDYRGSGG GYRGSGGFQR RGYGGGYFGQ GRGGGGGGGY
//
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