ID DHX9_HUMAN Reviewed; 1270 AA. AC Q08211; B2RNV4; Q05CI5; Q12803; Q32Q22; Q5VY62; Q6PD69; Q99556; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 4. DT 27-MAR-2024, entry version 239. DE RecName: Full=ATP-dependent RNA helicase A {ECO:0000305}; DE EC=3.6.4.13 {ECO:0000269|PubMed:11416126, ECO:0000269|PubMed:1537828, ECO:0000269|PubMed:20510246, ECO:0000269|PubMed:20669935, ECO:0000269|PubMed:24049074, ECO:0000269|PubMed:25062910, ECO:0000269|PubMed:8690889}; DE AltName: Full=DEAH box protein 9; DE AltName: Full=DExH-box helicase 9 {ECO:0000312|HGNC:HGNC:2750}; DE AltName: Full=Leukophysin {ECO:0000303|PubMed:8690889}; DE Short=LKP {ECO:0000303|PubMed:8690889}; DE AltName: Full=Nuclear DNA helicase II {ECO:0000303|PubMed:1537828, ECO:0000303|PubMed:8344961, ECO:0000303|PubMed:9111062}; DE Short=NDH II {ECO:0000303|PubMed:8344961, ECO:0000303|PubMed:9111062}; DE AltName: Full=RNA helicase A {ECO:0000303|PubMed:9111062}; GN Name=DHX9 {ECO:0000312|HGNC:HGNC:2750}; GN Synonyms=DDX9 {ECO:0000312|HGNC:HGNC:2750}, LKP, NDH2; 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 1), PARTIAL PROTEIN SEQUENCE, AND RP VARIANT VAL-894. RX PubMed=8344961; DOI=10.1016/s0021-9258(19)85490-x; RA Lee C.-G., Hurwitz J.; RT "Human RNA helicase A is homologous to the maleless protein of RT Drosophila."; RL J. Biol. Chem. 268:16822-16830(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION. RX PubMed=8690889; RA Abdelhaleem M.M., Hameed S., Klassen D., Greenberg A.H.; RT "Leukophysin: an RNA helicase A-related molecule identified in cytotoxic T RT cell granules and vesicles."; RL J. Immunol. 156:2026-2035(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN DNA/RNA UNWINDING, RP CATALYTIC ACTIVITY, DNA-BINDING, RNA-BINDING, AND DOMAIN DRBM. RX PubMed=9111062; DOI=10.1074/jbc.272.17.11487; RA Zhang S., Grosse F.; RT "Domain structure of human nuclear DNA helicase II (RNA helicase A)."; RL J. Biol. Chem. 272:11487-11494(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Muscle, 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 [8] RP PARTIAL PROTEIN SEQUENCE, FUNCTION IN TRANSCRIPTIONAL REGULATION, RP INTERACTION WITH SMN1; SMN COMPLEX AND RNA POLYMERASE II HOLOENZYME, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=11149922; DOI=10.1083/jcb.152.1.75; RA Pellizzoni L., Charroux B., Rappsilber J., Mann M., Dreyfuss G.; RT "A functional interaction between the survival motor neuron complex and RNA RT polymerase II."; RL J. Cell Biol. 152:75-85(2001). RN [9] RP FUNCTION IN DNA/RNA UNWINDING, CATALYTIC ACTIVITY, AND RNA-BINDING. RX PubMed=1537828; DOI=10.1016/s0021-9258(18)42849-9; RA Lee C.G., Hurwitz J.; RT "A new RNA helicase isolated from HeLa cells that catalytically RT translocates in the 3' to 5' direction."; RL J. Biol. Chem. 267:4398-4407(1992). RN [10] RP FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH CREBBP AND RNA RP POLYMERASE II HOLOENZYME, AND MUTAGENESIS OF LYS-417. RX PubMed=9323138; DOI=10.1016/s0092-8674(00)80376-1; RA Nakajima T., Uchida C., Anderson S.F., Lee C.-G., Hurwitz J., Parvin J.D., RA Montminy M.; RT "RNA helicase A mediates association of CBP with RNA polymerase II."; RL Cell 90:1107-1112(1997). RN [11] RP FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION, RNA-BINDING, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=9162007; DOI=10.1126/science.276.5317.1412; RA Tang H., Gaietta G.M., Fischer W.H., Ellisman M.H., Wong-Staal F.; RT "A cellular cofactor for the constitutive transport element of type D RT retrovirus."; RL Science 276:1412-1415(1997). RN [12] RP FUNCTION IN TRANSCRIPTIONAL REGULATION, AND INTERACTION WITH BRCA1. RX PubMed=9662397; DOI=10.1038/930; RA Anderson S.F., Schlegel B.P., Nakajima T., Wolpin E.S., Parvin J.D.; RT "BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RT RNA helicase A."; RL Nat. Genet. 19:254-256(1998). RN [13] RP SUBCELLULAR LOCATION, RNA-BINDING, AND DNA-BINDING. RX PubMed=10198287; DOI=10.1242/jcs.112.7.1055; RA Zhang S., Herrmann C., Grosse F.; RT "Pre-mRNA and mRNA binding of human nuclear DNA helicase II (RNA helicase RT A)."; RL J. Cell Sci. 112:1055-1064(1999). RN [14] RP SUBCELLULAR LOCATION, DOMAIN RGG, AND MUTAGENESIS OF LYS-1163 AND ARG-1166. RX PubMed=10207077; DOI=10.1128/mcb.19.5.3540; RA Tang H., McDonald D., Middlesworth T., Hope T.J., Wong-Staal F.; RT "The carboxyl terminus of RNA helicase A contains a bidirectional nuclear RT transport domain."; RL Mol. Cell. Biol. 19:3540-3550(1999). RN [15] RP FUNCTION (MICROBIAL INFECTION), AND RNA-BINDING (MICROBIAL INFECTION). RX PubMed=9892698; DOI=10.1073/pnas.96.2.709; RA Li J., Tang H., Mullen T.M., Westberg C., Reddy T.R., Rose D.W., RA Wong-Staal F.; RT "A role for RNA helicase A in post-transcriptional regulation of HIV type RT 1."; RL Proc. Natl. Acad. Sci. U.S.A. 96:709-714(1999). RN [16] RP FUNCTION IN MRNA EXPORT, AND INTERACTION WITH NXF1. RX PubMed=10924507; DOI=10.1074/jbc.m003933200; RA Tang H., Wong-Staal F.; RT "Specific interaction between RNA helicase A and Tap, two cellular proteins RT that bind to the constitutive transport element of type D retrovirus."; RL J. Biol. Chem. 275:32694-32700(2000). RN [17] RP FUNCTION IN TRANSCRIPTIONAL REGULATION, PROMOTER DNA-BINDING, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=11038348; DOI=10.1074/jbc.m004481200; RA Myoehaenen S., Baylin S.B.; RT "Sequence-specific DNA binding activity of RNA helicase A to the p16INK4a RT promoter."; RL J. Biol. Chem. 276:1634-1642(2001). RN [18] RP FUNCTION (MICROBIAL INFECTION), AND RNA-BINDING (MICROBIAL INFECTION). RX PubMed=11096080; DOI=10.1074/jbc.m006892200; RA Fujii R., Okamoto M., Aratani S., Oishi T., Ohshima T., Taira K., Baba M., RA Fukamizu A., Nakajima T.; RT "A role of RNA helicase A in cis-acting transactivation response element- RT mediated transcriptional regulation of human immunodeficiency virus type RT 1."; RL J. Biol. Chem. 276:5445-5451(2001). RN [19] RP FUNCTION IN MRNA EXPORT, RNA-BINDING, AND INTERACTION WITH AKAP8L. RX PubMed=11402034; DOI=10.1074/jbc.m102809200; RA Yang J.P., Tang H., Reddy T.R., Wong-Staal F.; RT "Mapping the functional domains of HAP95, a protein that binds RNA helicase RT A and activates the constitutive transport element of type D RT retroviruses."; RL J. Biol. Chem. 276:30694-30700(2001). RN [20] RP FUNCTION IN TRANSCRIPTIONAL REGULATION, CATALYTIC ACTIVITY, INTERACTION RP WITH RNA POLYMERASE II HOLOENZYME, ATP-BINDING, DOMAIN MTAD, AND RP MUTAGENESIS OF TRP-332; TRP-339 AND TRP-342. RX PubMed=11416126; DOI=10.1128/mcb.21.14.4460-4469.2001; RA Aratani S., Fujii R., Oishi T., Fujita H., Amano T., Ohshima T., RA Hagiwara M., Fukamizu A., Nakajima T.; RT "Dual roles of RNA helicase A in CREB-dependent transcription."; RL Mol. Cell. Biol. 21:4460-4469(2001). RN [21] RP FUNCTION, INTERACTION WITH ACTB AND HNRNPC, AND SUBCELLULAR LOCATION. RX PubMed=11687588; DOI=10.1074/jbc.m109393200; RA Zhang S., Buder K., Burkhardt C., Schlott B., Goerlach M., Grosse F.; RT "Nuclear DNA helicase II/RNA helicase A binds to filamentous actin."; RL J. Biol. Chem. 277:843-853(2002). RN [22] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271; RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., RA Greco A., Hochstrasser D.F., Diaz J.-J.; RT "Functional proteomic analysis of human nucleolus."; RL Mol. Biol. Cell 13:4100-4109(2002). RN [23] RP INTERACTION WITH ILF3. RX PubMed=12946349; DOI=10.1016/s0022-2836(03)00885-4; RA Reichman T.W., Parrott A.M., Fierro-Monti I., Caron D.J., Kao P.N., RA Lee C.G., Li H., Mathews M.B.; RT "Selective regulation of gene expression by nuclear factor 110, a member of RT the NF90 family of double-stranded RNA-binding proteins."; RL J. Mol. Biol. 332:85-98(2003). RN [24] RP FUNCTION IN TRANSCRIPTIONAL REGULATION, AND INTERACTION WITH MBD2. RX PubMed=12665568; DOI=10.1128/mcb.23.8.2645-2657.2003; RA Fujita H., Fujii R., Aratani S., Amano T., Fukamizu A., Nakajima T.; RT "Antithetic effects of MBD2a on gene regulation."; RL Mol. Cell. Biol. 23:2645-2657(2003). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [26] RP FUNCTION IN DNA/RNA UNWINDING, INTERACTION WITH TOP2A, AND DOUBLE-STRAND RP DNA-BINDING AND RNA-BINDING. RX PubMed=12711669; DOI=10.1093/nar/gkg328; RA Zhou K., Choe K.-T., Zaidi Z., Wang Q., Mathews M.B., Lee C.-G.; RT "RNA helicase A interacts with dsDNA and topoisomerase IIalpha."; RL Nucleic Acids Res. 31:2253-2260(2003). RN [27] RP FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH RELA, AND RP MUTAGENESIS OF LYS-417. RX PubMed=15355351; DOI=10.1111/j.1432-1033.2004.04314.x; RA Tetsuka T., Uranishi H., Sanda T., Asamitsu K., Yang J.-P., Wong-Staal F., RA Okamoto T.; RT "RNA helicase A interacts with nuclear factor kappaB p65 and functions as a RT transcriptional coactivator."; RL Eur. J. Biochem. 271:3741-3751(2004). RN [28] RP METHYLATION, INTERACTION WITH PRMT1, AND DOMAIN RGG. RX PubMed=15084609; DOI=10.1074/jbc.c300512200; RA Smith W.A., Schurter B.T., Wong-Staal F., David M.; RT "Arginine methylation of RNA helicase a determines its subcellular RT localization."; RL J. Biol. Chem. 279:22795-22798(2004). RN [29] RP INTERACTION WITH XRCC5, AND PHOSPHORYLATION BY PRKDC. RX PubMed=14704337; DOI=10.1093/nar/gkg933; RA Zhang S., Schlott B., Goerlach M., Grosse F.; RT "DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA helicase RT II/RNA helicase A and hnRNP proteins in an RNA-dependent manner."; RL Nucleic Acids Res. 32:1-10(2004). RN [30] RP INTERACTION WITH H2AX. RX PubMed=15613478; DOI=10.1074/jbc.m411444200; RA Mischo H.E., Hemmerich P., Grosse F., Zhang S.; RT "Actinomycin D induces histone gamma-H2AX foci and complex formation of RT gamma-H2AX with Ku70 and nuclear DNA helicase II."; RL J. Biol. Chem. 280:9586-9594(2005). RN [31] RP INTERACTION WITH WRN. RX PubMed=15995249; DOI=10.1074/jbc.m503882200; RA Friedemann J., Grosse F., Zhang S.; RT "Nuclear DNA helicase II (RNA helicase A) interacts with Werner syndrome RT helicase and stimulates its exonuclease activity."; RL J. Biol. Chem. 280:31303-31313(2005). RN [32] RP SUBCELLULAR LOCATION, INTERACTION WITH THE IMPORTIN COMPLEX, NUCLEAR RP LOCALIZATION SIGNAL, AND MUTAGENESIS OF ARG-1160; LYS-1163 AND ARG-1166. RX PubMed=16375861; DOI=10.1016/j.bbrc.2005.11.161; RA Aratani S., Oishi T., Fuj ita H., Nakazawa M., Fujii R., Imamoto N., RA Yoneda Y., Fukamizu A., Nakajima T.; RT "The nuclear import of RNA helicase A is mediated by importin-alpha3."; RL Biochem. Biophys. Res. Commun. 340:125-133(2006). RN [33] RP FUNCTION IN VIRAL MRNA TRANSLATION (MICROBIAL INFECTION), FUNCTION IN MRNA RP TRANSLATION, ASSOCIATION WITH POLYRIBOSOMES, RNA-BINDING (MICROBIAL RP INFECTION), RNA-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16680162; DOI=10.1038/nsmb1092; RA Hartman T.R., Qian S., Bolinger C., Fernandez S., Schoenberg D.R., RA Boris-Lawrie K.; RT "RNA helicase A is necessary for translation of selected messenger RNAs."; RL Nat. Struct. Mol. Biol. 13:509-516(2006). RN [34] RP INTERACTION WITH SP7, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS RP SPECTROMETRY. 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 helicase RT A."; RL Biochem. Biophys. Res. Commun. 355:347-351(2007). RN [35] RP INTERACTION WITH H2AX, AND SUBCELLULAR LOCATION. RX PubMed=17498979; DOI=10.1016/j.cellbi.2007.03.027; RA Zhang S., Hemmerich P., Grosse F.; RT "Werner syndrome helicase (WRN), nuclear DNA helicase II (NDH II) and RT histone gammaH2AX are localized to the centrosome."; RL Cell Biol. Int. 31:1109-1121(2007). RN [36] 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-dependent RT protein kinase, poly(ADP-ribose) polymerase, and RNA helicase A."; RL J. Biol. Chem. 282:9983-9995(2007). RN [37] RP FUNCTION IN RISC LOADING COMPLEX, ASSOCIATION WITH THE RISC LOADING RP COMPLEX, INTERACTION WITH AGO2; DICER1 AND TARBP2, AND MUTAGENESIS OF RP LYS-417. RX PubMed=17531811; DOI=10.1016/j.molcel.2007.04.016; RA Robb G.B., Rana T.M.; RT "RNA helicase A interacts with RISC in human cells and functions in RISC RT loading."; RL Mol. Cell 26:523-537(2007). RN [38] RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, AND RP SUBCELLULAR LOCATION. RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200; RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., RA Johnsen A.H., Christiansen J., Nielsen F.C.; RT "Molecular composition of IMP1 ribonucleoprotein granules."; RL Mol. Cell. Proteomics 6:798-811(2007). RN [39] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [40] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [41] RP FUNCTION, FUNCTION (MICROBIAL INFECTION), INTERACTION WITH EIF2AK2, AND RP PHOSPHORYLATION BY EIF2AK2. 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 helicase RT A."; RL PLoS Pathog. 5:E1000311-E1000311(2009). RN [42] RP FUNCTION IN MRNA STABILITY, COMPONENT OF THE CRD-MEDIATED MRNA RP STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=19029303; DOI=10.1261/rna.1175909; RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., RA Buchmeier S., Wahle E., Huettelmaiery S.; RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."; RL RNA 15:104-115(2009). RN [43] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191; LYS-199 AND LYS-1024, AND RP IDENTIFICATION BY MASS 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 [44] RP FUNCTION AS A TRIPLEX DNA HELICASE, FUNCTION IN DNA REPLICATION, AND RP CATALYTIC ACTIVITY. RX PubMed=20669935; DOI=10.1021/bi100795m; RA Jain A., Bacolla A., Chakraborty P., Grosse F., Vasquez K.M.; RT "Human DHX9 helicase unwinds triple-helical DNA structures."; RL Biochemistry 49:6992-6999(2010). RN [45] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH MYD88, MICROBIAL RP DNA-BINDING (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RX PubMed=20696886; DOI=10.1073/pnas.1006539107; RA Kim T., Pazhoor S., Bao M., Zhang Z., Hanabuchi S., Facchinetti V., RA Bover L., Plumas J., Chaperot L., Qin J., Liu Y.J.; RT "Aspartate-glutamate-alanine-histidine box motif (DEAH)/RNA helicase A RT helicases sense microbial DNA in human plasmacytoid dendritic cells."; RL Proc. Natl. Acad. Sci. U.S.A. 107:15181-15186(2010). RN [46] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION BY RP 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 [47] 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 [48] RP FUNCTION IN DNA/RNA UNWINDING, AND CATALYTIC ACTIVITY. RX PubMed=21561811; DOI=10.1016/j.dnarep.2011.04.013; RA Chakraborty P., Grosse F.; RT "Human DHX9 helicase preferentially unwinds RNA-containing displacement RT loops (R-loops) and G-quadruplexes."; RL DNA Repair 10:654-665(2011). RN [49] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH MAVS, AND DOUBLE STRANDED RP RNA-BINDING (MICROBIAL INFECTION). RX PubMed=21957149; DOI=10.4049/jimmunol.1101307; RA Zhang Z., Yuan B., Lu N., Facchinetti V., Liu Y.J.; RT "DHX9 pairs with IPS-1 to sense double-stranded RNA in myeloid dendritic RT cells."; RL J. Immunol. 187:4501-4508(2011). RN [50] RP FUNCTION IN MRNA TRANSLATION, AND INTERACTION WITH LIN28A. RX PubMed=21247876; DOI=10.1093/nar/gkq1350; RA Jin J., Jing W., Lei X.X., Feng C., Peng S., Boris-Lawrie K., Huang Y.; RT "Evidence that Lin28 stimulates translation by recruiting RNA helicase A to RT polysomes."; RL Nucleic Acids Res. 39:3724-3734(2011). RN [51] RP FUNCTION IN MRNA TRANSLATION, INTERACTION WITH LARP6, MRNA-BINDING, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22190748; DOI=10.1261/rna.030288.111; RA Manojlovic Z., Stefanovic B.; RT "A novel role of RNA helicase A in regulation of translation of type I RT collagen mRNAs."; RL RNA 18:321-334(2012). RN [52] RP INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3. RX PubMed=23640942; DOI=10.1515/hsz-2013-0111; RA Wachter K., Kohn M., Stohr N., Huttelmaier S.; RT "Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding RT proteins) is modulated by distinct RNA-binding domains."; RL Biol. Chem. 394:1077-1090(2013). RN [53] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-321; SER-449 AND RP SER-506, AND 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 [54] RP INTERACTION WITH MCM3AP. RX PubMed=23652018; DOI=10.1038/ncomms2823; RA Singh S.K., Maeda K., Eid M.M., Almofty S.A., Ono M., Pham P., RA Goodman M.F., Sakaguchi N.; RT "GANP regulates recruitment of AID to immunoglobulin variable regions by RT modulating transcription and nucleosome occupancy."; RL Nat. Commun. 4:1830-1830(2013). RN [55] RP FUNCTION AS A TRIPLEX DNA HELICASE, CATALYTIC ACTIVITY, AND TRIPLEX RP DNA-BINDING. RX PubMed=24049074; DOI=10.1093/nar/gkt804; RA Jain A., Bacolla A., Del Mundo I.M., Zhao J., Wang G., Vasquez K.M.; RT "DHX9 helicase is involved in preventing genomic instability induced by RT alternatively structured DNA in human cells."; RL Nucleic Acids Res. 41:10345-10357(2013). RN [56] RP INTERACTION WITH LMX1B, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=23308148; DOI=10.1371/journal.pone.0053122; RA Hoekstra E.J., Mesman S., de Munnik W.A., Smidt M.P.; RT "LMX1B is part of a transcriptional complex with PSPC1 and PSF."; RL PLoS ONE 8:E53122-E53122(2013). RN [57] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=25149208; DOI=10.1016/j.bbagrm.2014.08.008; RA Xing L., Niu M., Kleiman L.; RT "Role of the OB-fold of RNA helicase A in the synthesis of HIV-1 RNA."; RL Biochim. Biophys. Acta 1839:1069-1078(2014). RN [58] RP FUNCTION IN DNA/RNA UNWINDING, CATALYTIC ACTIVITY, AND DOMAINS. RX PubMed=25062910; DOI=10.1016/j.bbapap.2014.07.001; RA Xing L., Zhao X., Niu M., Kleiman L.; RT "Helicase associated 2 domain is essential for helicase activity of RNA RT helicase A."; RL Biochim. Biophys. Acta 1844:1757-1764(2014). RN [59] RP FUNCTION IN DNA REPLICATION, CHROMATIN-BINDING, AND MUTAGENESIS OF ASP-511; RP GLU-512 AND SER-543. RX PubMed=24990949; DOI=10.1074/jbc.m114.568535; RA Lee T., Di Paola D., Malina A., Mills J.R., Kreps A., Grosse F., Tang H., RA Zannis-Hadjopoulos M., Larsson O., Pelletier J.; RT "Suppression of the DHX9 helicase induces premature senescence in human RT diploid fibroblasts in a p53-dependent manner."; RL J. Biol. Chem. 289:22798-22814(2014). RN [60] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, 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 [61] RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-146 AND ARG-1175, AND RP IDENTIFICATION BY MASS 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 [62] RP FUNCTION (MICROBIAL INFECTION), AND RNA-BINDING (MICROBIAL INFECTION). RX PubMed=27107641; DOI=10.1016/j.jmb.2016.04.011; RA Boeras I., Song Z., Moran A., Franklin J., Brown W.C., Johnson M., RA Boris-Lawrie K., Heng X.; RT "DHX9/RHA binding to the PBS-segment of the genomic RNA during HIV-1 RT assembly bolsters virion infectivity."; RL J. Mol. Biol. 428:2418-2429(2016). RN [63] RP FUNCTION IN POST-TRANSCRIPTIONAL PROCESSING, INTERACTION WITH NUP98, RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS RP OF ILE-347 AND LYS-417. RX PubMed=28221134; DOI=10.7554/elife.18825; RA Capitanio J.S., Montpetit B., Wozniak R.W.; RT "Human Nup98 regulates the localization and activity of DExH/D-box helicase RT DHX9."; RL Elife 6:0-0(2017). RN [64] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-697, 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 [65] RP FUNCTION IN POST-TRANSCRIPTIONAL PROCESSING, INTERACTION WITH ADAR, AND ALU RP RNA-BINDING. RX PubMed=28355180; DOI=10.1038/nature21715; RA Aktas T., Avsar Ilik I., Maticzka D., Bhardwaj V., Pessoa Rodrigues C., RA Mittler G., Manke T., Backofen R., Akhtar A.; RT "DHX9 suppresses RNA processing defects originating from the Alu invasion RT of the human genome."; RL Nature 544:115-119(2017). RN [66] RP FUNCTION, AND INTERACTION WITH NLRP9. 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 epithelial RT cells."; RL Nature 546:667-670(2017). RN [67] RP INTERACTION WITH CHIKUNGUNYA VIRUS NON-STRUCTURAL PROTEIN 3 (MICROBIAL RP INFECTION). RX PubMed=30463980; DOI=10.1128/jvi.01764-18; RA Matkovic R., Bernard E., Fontanel S., Eldin P., Chazal N., Hassan Hersi D., RA Merits A., Peloponese J.M. Jr., Briant L.; RT "The Host DHX9 DExH-Box Helicase Is Recruited to Chikungunya Virus RT Replication Complexes for Optimal Genomic RNA Translation."; RL J. Virol. 93:0-0(2019). RN [68] RP INTERACTION WITH EPSTEIN BARR VIRUS MRNA EXPORT FACTOR ICP27 HOMOLOG RP (MICROBIAL INFECTION). RX PubMed=30541834; DOI=10.1128/jvi.01244-18; RA Fu W., Verma D., Burton A., Swaminathan S.; RT "Cellular RNA Helicase DHX9 Interacts with the Essential Epstein-Barr Virus RT (EBV) Protein SM and Restricts EBV Lytic Replication."; RL J. Virol. 93:0-0(2019). RN [69] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 329-563 IN COMPLEX WITH ADP AND RP MANGANESE, NUCLEOTIDE-BINDING, AND CATALYTIC ACTIVITY. RX PubMed=20510246; DOI=10.1016/j.jmb.2010.05.046; RA Schutz P., Wahlberg E., Karlberg T., Hammarstrom M., Collins R., Flores A., RA Schuler H.; RT "Crystal structure of human RNA helicase A (DHX9): structural basis for RT unselective nucleotide base binding in a DEAD-box variant protein."; RL J. Mol. Biol. 400:768-782(2010). RN [70] RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-86 AND 169-263 IN COMPLEX WITH RP SIRNA, DOUBLE-STRANDED RNA-BINDING, INTERACTION WITH AGO2 AND TARBP2, AND RP MUTAGENESIS OF LYS-5; ASN-6; TYR-9; ASN-30; ASN-53; LYS-54; LYS-55; RP LYS-182; ASN-186; GLN-187; HIS-207; ASN-234; LYS-235 AND LYS-236. RX PubMed=23361462; DOI=10.1093/nar/gkt042; RA Fu Q., Yuan Y.A.; RT "Structural insights into RISC assembly facilitated by dsRNA-binding RT domains of human RNA helicase A (DHX9)."; RL Nucleic Acids Res. 41:3457-3470(2013). CC -!- FUNCTION: Multifunctional ATP-dependent nucleic acid helicase that CC unwinds DNA and RNA in a 3' to 5' direction and that plays important CC roles in many processes, such as DNA replication, transcriptional CC activation, post-transcriptional RNA regulation, mRNA translation and CC RNA-mediated gene silencing (PubMed:9111062, PubMed:11416126, CC PubMed:12711669, PubMed:15355351, PubMed:16680162, PubMed:17531811, CC PubMed:20669935, PubMed:21561811, PubMed:24049074, PubMed:25062910, CC PubMed:24990949, PubMed:28221134). Requires a 3'-single-stranded tail CC as entry site for acid nuclei unwinding activities as well as the CC binding and hydrolyzing of any of the four ribo- or deoxyribo- CC nucleotide triphosphates (NTPs) (PubMed:1537828). Unwinds numerous CC nucleic acid substrates such as double-stranded (ds) DNA and RNA, CC DNA:RNA hybrids, DNA and RNA forks composed of either partially CC complementary DNA duplexes or DNA:RNA hybrids, respectively, and also CC DNA and RNA displacement loops (D- and R-loops), triplex-helical DNA CC (H-DNA) structure and DNA and RNA-based G-quadruplexes CC (PubMed:20669935, PubMed:21561811, PubMed:24049074). Binds dsDNA, CC single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing RNA CC (PubMed:9111062, PubMed:10198287). Binds also to circular dsDNA or CC dsRNA of either linear and/or circular forms and stimulates the CC relaxation of supercoiled DNAs catalyzed by topoisomerase TOP2A CC (PubMed:12711669). Plays a role in DNA replication at origins of CC replication and cell cycle progression (PubMed:24990949). Plays a role CC as a transcriptional coactivator acting as a bridging factor between CC polymerase II holoenzyme and transcription factors or cofactors, such CC as BRCA1, CREBBP, RELA and SMN1 (PubMed:11149922, PubMed:9323138, CC PubMed:9662397, PubMed:11038348, PubMed:11416126, PubMed:15355351, CC PubMed:28221134). Binds to the CDKN2A promoter (PubMed:11038348). Plays CC several roles in post-transcriptional regulation of gene expression CC (PubMed:28221134, PubMed:28355180). In cooperation with NUP98, promotes CC pre-mRNA alternative splicing activities of a subset of genes CC (PubMed:11402034, PubMed:16680162, PubMed:28221134, PubMed:28355180). CC As component of a large PER complex, is involved in the negative CC regulation of 3' transcriptional termination of circadian target genes CC such as PER1 and NR1D1 and the control of the circadian rhythms (By CC similarity). Acts also as a nuclear resolvase that is able to bind and CC neutralize harmful massive secondary double-stranded RNA structures CC formed by inverted-repeat Alu retrotransposon elements that are CC inserted and transcribed as parts of genes during the process of gene CC transposition (PubMed:28355180). Involved in the positive regulation of CC nuclear export of constitutive transport element (CTE)-containing CC unspliced mRNA (PubMed:9162007, PubMed:10924507, PubMed:11402034). CC Component of the coding region determinant (CRD)-mediated complex that CC promotes cytoplasmic MYC mRNA stability (PubMed:19029303). Plays a role CC in mRNA translation (PubMed:28355180). Positively regulates translation CC of selected mRNAs through its binding to post-transcriptional control CC element (PCE) in the 5'-untranslated region (UTR) (PubMed:16680162). CC Involved with LARP6 in the translation stimulation of type I collagen CC mRNAs for CO1A1 and CO1A2 through binding of a specific stem-loop CC structure in their 5'-UTRs (PubMed:22190748). Stimulates LIN28A- CC dependent mRNA translation probably by facilitating ribonucleoprotein CC remodeling during the process of translation (PubMed:21247876). Plays CC also a role as a small interfering (siRNA)-loading factor involved in CC the RNA-induced silencing complex (RISC) loading complex (RLC) CC assembly, and hence functions in the RISC-mediated gene silencing CC process (PubMed:17531811). Binds preferentially to short double- CC stranded RNA, such as those produced during rotavirus intestinal CC infection (PubMed:28636595). This interaction may mediate NLRP9 CC inflammasome activation and trigger inflammatory response, including CC IL18 release and pyroptosis (PubMed:28636595). Finally, mediates the CC attachment of heterogeneous nuclear ribonucleoproteins (hnRNPs) to CC actin filaments in the nucleus (PubMed:11687588). CC {ECO:0000250|UniProtKB:O70133, ECO:0000269|PubMed:10198287, CC ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:11038348, CC ECO:0000269|PubMed:11149922, ECO:0000269|PubMed:11402034, CC ECO:0000269|PubMed:11416126, ECO:0000269|PubMed:11687588, CC ECO:0000269|PubMed:12711669, ECO:0000269|PubMed:15355351, CC ECO:0000269|PubMed:1537828, ECO:0000269|PubMed:16680162, CC ECO:0000269|PubMed:17531811, ECO:0000269|PubMed:19029303, CC ECO:0000269|PubMed:20669935, ECO:0000269|PubMed:21247876, CC ECO:0000269|PubMed:21561811, ECO:0000269|PubMed:22190748, CC ECO:0000269|PubMed:24049074, ECO:0000269|PubMed:24990949, CC ECO:0000269|PubMed:25062910, ECO:0000269|PubMed:28221134, CC ECO:0000269|PubMed:28355180, ECO:0000269|PubMed:28636595, CC ECO:0000269|PubMed:9111062, ECO:0000269|PubMed:9162007, CC ECO:0000269|PubMed:9323138, ECO:0000269|PubMed:9662397}. CC -!- FUNCTION: (Microbial infection) Plays a role in HIV-1 replication and CC virion infectivity (PubMed:11096080, PubMed:19229320, PubMed:25149208, CC PubMed:27107641). Enhances HIV-1 transcription by facilitating the CC binding of RNA polymerase II holoenzyme to the proviral DNA CC (PubMed:11096080, PubMed:25149208). Binds (via DRBM domain 2) to the CC HIV-1 TAR RNA and stimulates HIV-1 transcription of transactivation CC response element (TAR)-containing mRNAs (PubMed:9892698, CC PubMed:11096080). Involved also in HIV-1 mRNA splicing and transport CC (PubMed:25149208). Positively regulates HIV-1 gag mRNA translation, CC through its binding to post-transcriptional control element (PCE) in CC the 5'-untranslated region (UTR) (PubMed:16680162). Binds (via DRBM CC domains) to a HIV-1 double-stranded RNA region of the primer binding CC site (PBS)-segment of the 5'-UTR, and hence stimulates DHX9 CC incorporation into virions and virion infectivity (PubMed:27107641). CC Also plays a role as a cytosolic viral MyD88-dependent DNA and RNA CC sensors in plasmacytoid dendritic cells (pDCs), and hence induce CC antiviral innate immune responses (PubMed:20696886, PubMed:21957149). CC Binds (via the OB-fold region) to viral single-stranded DNA CC unmethylated C-phosphate-G (CpG) oligonucleotide (PubMed:20696886). CC {ECO:0000269|PubMed:11096080, ECO:0000269|PubMed:16680162, CC ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:20696886, CC ECO:0000269|PubMed:21957149, ECO:0000269|PubMed:25149208, CC ECO:0000269|PubMed:27107641, ECO:0000269|PubMed:9892698}. 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:11416126, ECO:0000269|PubMed:1537828, CC ECO:0000269|PubMed:20510246, ECO:0000269|PubMed:20669935, CC ECO:0000269|PubMed:24049074, ECO:0000269|PubMed:25062910, CC ECO:0000269|PubMed:8690889}; CC -!- SUBUNIT: Component of the coding region determinant (CRD)-mediated CC complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1 CC (PubMed:19029303). Identified in a mRNP complex, at least composed of CC DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, CC STAU1, STAU2, SYNCRIP and YBX1 (PubMed:19029303). Identified in a CC IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs CC (PubMed:17289661). The large PER complex involved in the repression of CC transcriptional termination is composed of at least PER2, CDK9, DDX5, CC DHX9, NCBP1 and POLR2A (active) (By similarity). Associates (via DRBM CC domains) with the RISC complex; this association occurs in a small CC interfering (siRNA)-dependent manner (PubMed:17531811, CC PubMed:23361462). Associates with the SMN complex; this association CC induces recruitment of DHX9 to the RNA polymerase II (ref.8). CC Associates with polysomes in a LIN28A-dependent manner CC (PubMed:16680162, PubMed:21247876). Interacts (via C-terminus) with CC ACTB; this interaction is direct and mediates the attachment to nuclear CC ribonucleoprotein complexes (PubMed:11687588). Interacts with ADAR CC isoform 1; this interaction occurs in a RNA-independent manner CC (PubMed:28355180). Interacts (via DRBM domains) with AGO2 (via middle CC region); this interaction promotes active RISC assembly by promoting CC the association of siRNA with AGO2 (PubMed:17531811, PubMed:23361462). CC Interacts (via RGG region) with AKAP8L (via N-terminus) CC (PubMed:11402034). Interacts with BRCA1 (via C-terminus); this CC interaction is direct and links BRCA1 to the RNA polymerase II CC holoenzyme (PubMed:9662397). Interacts (via N-terminus) with CREBBP; CC this interaction mediates association with RNA polymerase II holoenzyme CC and stimulates CREB-dependent transcriptional activation CC (PubMed:9323138). 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 (PubMed:17531811). Interacts with H2AX; this interaction is direct, CC requires phosphorylation of histone H2AX on 'Ser-140' by PRKDC and CC promotes binding of DHX9 to transcriptionally stalled sites on CC chromosomal DNA in response to genotoxic stress (PubMed:15613478, CC PubMed:17498979). Interacts with HNRNPC; this interaction is direct, CC enhanced probably by their concomitant binding to RNA and mediates the CC attachment to actin filaments (PubMed:11687588). Interacts (via RGG CC region) with PRMT1 (PubMed:15084609). Interacts with IGF2BP1 CC (PubMed:17289661, PubMed:23640942). Interacts with IGF2BP2, IGF2BP3 CC (PubMed:23640942). Interacts (via DRBM domains) with ILF3; this CC interaction occurs in a RNA-independent manner (PubMed:12946349). CC Interacts with Importin alpha/Importin beta receptor (PubMed:16375861). CC Interacts with LARP6 (via C-terminus); this interaction occurs in a CC mRNA-independent manner (PubMed:22190748). Interacts (via N- and C- CC terminus) with LIN28A (via C-terminus); this interaction occurs in a CC RNA-independent manner (PubMed:21247876). Interacts with LMX1B CC (PubMed:23308148). Interacts (via helicase C-terminal domain, HA2 and CC OB-fold regions) with MAVS (via CARD domain); this interaction occurs CC in both resting and double-stranded RNA poly(I:C)-induced cells CC (PubMed:21957149). Interacts with MBD2; this interaction stimulates CC transcriptional activation in a CREB-dependent manner CC (PubMed:12665568). Interacts (via H2A and OB-fold regions) with MYD88 CC (via TIR domain); this interaction is direct (PubMed:20696886). CC Interacts with NLRP9 upon rotavirus infection; this interaction may CC trigger NLRP9 inflammasome activation and inflammatory response CC (PubMed:28636595). Interacts (via DRBM, OB-fold and RGG regions) with CC NUP98 (via N-terminus); this interaction occurs in a RNA-dependent CC manner and stimulates DHX9-mediated ATPase activity and regulates CC transcription and splicing of a subset of genes (PubMed:28221134). CC Interacts (via N-terminus) with NXF1 (via N-terminus); this interaction CC is direct and negatively regulates NXF1-mediated nuclear export of CC constitutive transport element (CTE)-containing cellular mRNAs CC (PubMed:10924507). Interacts with RELA; this interaction is direct and CC activates NF-kappa-B-mediated transcription (PubMed:15355351). CC Interacts (via MTAD region) with RNA polymerase II holoenzyme; this CC interaction stimulates transcription activation in a CREB-dependent CC manner (PubMed:11149922, PubMed:9323138, PubMed:11416126). Interacts CC (via RGG region) with SMN1; this interaction links SMN1 to the RNA CC polymerase II holoenzyme (PubMed:11149922). Interacts with SP7 CC (PubMed:17303075). Interacts (via DRBM domains) with TARBP2 (via DRBM CC first and second domains); this interaction occurs in a small CC interfering (siRNA)-dependent manner (PubMed:17531811, CC PubMed:23361462). Interacts with TOP2A; this interaction occurs in a E2 CC enzyme UBE2I- and RNA-dependent manner, negatively regulates DHX9- CC mediated double-stranded DNA and RNA duplex helicase activity and CC stimulates TOP2A-mediated supercoiled DNA relaxation activity CC (PubMed:12711669). Interacts (via DRBM domains and C-terminus) with WRN CC (via 3'-5' exonuclease domain); this interaction inhibits the DNA- CC dependent NTPase and DNA helicase activities of DHX9 and stimulates the CC 3'-5' exonuclease activity of WRN (PubMed:15995249). Interacts with CC XRCC5; this interaction occurs in a RNA-dependent manner CC (PubMed:14704337). Interacts with ZIC2 (via C2H2-type domain 3) CC (PubMed:17251188). Interacts with MCM3AP isoform GANP CC (PubMed:23652018). {ECO:0000250|UniProtKB:O70133, CC ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:11149922, CC ECO:0000269|PubMed:11402034, ECO:0000269|PubMed:11416126, CC ECO:0000269|PubMed:11687588, ECO:0000269|PubMed:12665568, CC ECO:0000269|PubMed:12711669, ECO:0000269|PubMed:12946349, CC ECO:0000269|PubMed:14704337, ECO:0000269|PubMed:15084609, CC ECO:0000269|PubMed:15355351, ECO:0000269|PubMed:15613478, CC ECO:0000269|PubMed:15995249, ECO:0000269|PubMed:16375861, CC ECO:0000269|PubMed:16680162, ECO:0000269|PubMed:17251188, CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17303075, CC ECO:0000269|PubMed:17498979, ECO:0000269|PubMed:17531811, CC ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19229320, CC ECO:0000269|PubMed:20696886, ECO:0000269|PubMed:21247876, CC ECO:0000269|PubMed:21957149, ECO:0000269|PubMed:22190748, CC ECO:0000269|PubMed:23308148, ECO:0000269|PubMed:23361462, CC ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:23652018, CC ECO:0000269|PubMed:28221134, ECO:0000269|PubMed:28355180, CC ECO:0000269|PubMed:28636595, ECO:0000269|PubMed:9323138, CC ECO:0000269|PubMed:9662397}. CC -!- SUBUNIT: (Microbial infection) Interacts with Chikungunya virus non- CC structural protein 3 (via C-terminus); this interaction allows the CC recruitment of DHX9 to the plasma membrane, where it associates with CC viral replication complexes and may play a role in the translation-to- CC replication switch. {ECO:0000269|PubMed:30463980}. CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus (EBV) CC mRNA export factor ICP27 homolog/SM protein; this interaction may have CC an inhibitory effect on virion production. CC {ECO:0000269|PubMed:30541834}. CC -!- INTERACTION: CC Q08211; P19525: EIF2AK2; NbExp=2; IntAct=EBI-352022, EBI-640775; CC Q08211; Q9UBU9: NXF1; NbExp=8; IntAct=EBI-352022, EBI-398874; CC Q08211; Q99873: PRMT1; NbExp=2; IntAct=EBI-352022, EBI-78738; CC Q08211; Q04206: RELA; NbExp=4; IntAct=EBI-352022, EBI-73886; CC Q08211; O14980: XPO1; NbExp=3; IntAct=EBI-352022, EBI-355867; CC Q08211; P67809: YBX1; NbExp=10; IntAct=EBI-352022, EBI-354065; CC Q08211; Q9HA38: ZMAT3; NbExp=3; IntAct=EBI-352022, EBI-2548480; CC Q08211; PRO_0000038050 [P19712]; Xeno; NbExp=6; IntAct=EBI-352022, EBI-10901281; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10198287, CC ECO:0000269|PubMed:10207077, ECO:0000269|PubMed:11687588, CC ECO:0000269|PubMed:16375861, ECO:0000269|PubMed:17303075, CC ECO:0000269|PubMed:9162007}. Nucleus, nucleoplasm CC {ECO:0000269|PubMed:28221134}. Nucleus, nucleolus CC {ECO:0000269|PubMed:12429849}. Cytoplasm {ECO:0000269|PubMed:10198287, CC ECO:0000269|PubMed:10207077, ECO:0000269|PubMed:16375861, CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:19029303, CC ECO:0000269|PubMed:20696886, ECO:0000269|PubMed:8690889, CC ECO:0000269|PubMed:9162007}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:14654843, CC ECO:0000269|PubMed:17498979}. Note=Nucleoplasmic shuttling protein CC (PubMed:10198287, PubMed:16375861, PubMed:10207077, PubMed:9162007). CC Its nuclear import involves the nucleocytoplasmic transport receptor CC Importin alpha/Importin beta receptor pathway in a Ran-dependent manner CC (PubMed:16375861). In interphase, localizes in nuclear stress granules CC and at perichromatin fibrils and in cytoplasmic ribonucleoprotein CC granules (PubMed:10198287). Colocalizes with WRN and H2AX at CC centrosomes in a microtubule-dependent manner following DNA damaging CC agent treatment (PubMed:17498979). Excluded from the mitotic nucleus as CC early as prophase and re-entered the nucleus at telophase CC (PubMed:10198287). Recruited in diffuse and discrete intranuclear foci CC (GLFG-body) in a NUP98-dependent manner (PubMed:28221134). Colocalizes CC with SP7 in the nucleus (PubMed:17303075). Colocalizes with ACTB at CC nuclear actin filaments inside the nucleus or at the nuclear pore CC (PubMed:11687588). Colocalizes with HNRNPC at nuclear ribonucleoprotein CC complex proteins in the nucleus (PubMed:11687588). Localized in CC cytoplasmic mRNP granules containing untranslated mRNAs CC (PubMed:17289661). {ECO:0000269|PubMed:10198287, CC ECO:0000269|PubMed:10207077, ECO:0000269|PubMed:11687588, CC ECO:0000269|PubMed:16375861, ECO:0000269|PubMed:17289661, CC ECO:0000269|PubMed:17303075, ECO:0000269|PubMed:17498979, CC ECO:0000269|PubMed:28221134, ECO:0000269|PubMed:9162007}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q08211-1; Sequence=Displayed; CC Name=2; Synonyms=Leukophysin, LKP; CC IsoId=Q08211-2; Sequence=VSP_042314; CC -!- DOMAIN: DRBM domains cooperate for the binding to nucleic acid but not CC for unwinding helicase activity (PubMed:9111062, PubMed:25062910). The CC helicase-associated domain-2 (HA2) region is essential for the duplex CC RNA unwinding helicase activity (PubMed:25062910). The minimal CC transactivation region (MTAD) mediates interaction with the RNA CC polymerase II holoenzyme and stimulates transcriptional activation in a CC CREB-dependent manner (PubMed:11416126). The oligonucleotide- or CC oligosaccharide-binding (OB-fold) and the repeated arginine and CC glycine-glycine (RGG) regions are dispensable for both RNA-binding and CC unwinding helicase activities (PubMed:25062910). The RGG region CC contains both nuclear localization signal (NLS) and nuclear export CC signal (NES) and is necessary and sufficient for nucleocytoplasmic CC shuttling in a RNA-independent manner (PubMed:10207077, CC PubMed:11149922). {ECO:0000269|PubMed:10207077, CC ECO:0000269|PubMed:11149922, ECO:0000269|PubMed:11416126, CC ECO:0000269|PubMed:25062910, ECO:0000269|PubMed:9111062}. CC -!- PTM: Methylated (PubMed:15084609). PRMT1-mediated methylation of CC undefined Arg residues in the RGG region is required for nuclear import CC of DHX9 (PubMed:15084609). {ECO:0000269|PubMed:15084609}. CC -!- PTM: Phosphorylated by PRKDC; phosphorylation occurs in a RNA-dependent CC manner (PubMed:14704337). Phosphorylated by EIF2AK2/PKR; this CC phosphorylation reduces its association with double-stranded RNA CC (PubMed:19229320). {ECO:0000269|PubMed:14704337, CC ECO:0000269|PubMed:19229320}. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44879/DHX9"; 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; L13848; AAB48855.1; -; mRNA. DR EMBL; U03643; AAA03571.1; -; mRNA. DR EMBL; Y10658; CAA71668.1; -; mRNA. DR EMBL; AB451248; BAG70062.1; -; mRNA. DR EMBL; AB451372; BAG70186.1; -; mRNA. DR EMBL; AL355999; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL662837; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471067; EAW91138.1; -; Genomic_DNA. DR EMBL; BC025245; AAH25245.1; -; mRNA. DR EMBL; BC058896; AAH58896.1; -; mRNA. DR EMBL; BC107881; AAI07882.1; -; mRNA. DR EMBL; BC137136; AAI37137.1; -; mRNA. DR CCDS; CCDS41444.1; -. [Q08211-1] DR RefSeq; NP_001348.2; NM_001357.4. [Q08211-1] DR PDB; 3LLM; X-ray; 2.80 A; A/B=329-563. DR PDB; 3VYX; X-ray; 2.29 A; A=152-264. DR PDB; 3VYY; X-ray; 2.90 A; A/B=1-91. DR PDB; 8SZP; X-ray; 2.62 A; A/B=149-1150. DR PDBsum; 3LLM; -. DR PDBsum; 3VYX; -. DR PDBsum; 3VYY; -. DR PDBsum; 8SZP; -. DR AlphaFoldDB; Q08211; -. DR BMRB; Q08211; -. DR SMR; Q08211; -. DR BioGRID; 108025; 606. DR ComplexPortal; CPX-1080; CRD-mediated mRNA stability complex. DR CORUM; Q08211; -. DR DIP; DIP-31504N; -. DR IntAct; Q08211; 157. DR MINT; Q08211; -. DR STRING; 9606.ENSP00000356520; -. DR GlyCosmos; Q08211; 2 sites, 1 glycan. DR GlyGen; Q08211; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q08211; -. DR MetOSite; Q08211; -. DR PhosphoSitePlus; Q08211; -. DR SwissPalm; Q08211; -. DR BioMuta; DHX9; -. DR DMDM; 116241330; -. DR CPTAC; CPTAC-355; -. DR CPTAC; CPTAC-356; -. DR EPD; Q08211; -. DR jPOST; Q08211; -. DR MassIVE; Q08211; -. DR MaxQB; Q08211; -. DR PaxDb; 9606-ENSP00000356520; -. DR PeptideAtlas; Q08211; -. DR ProteomicsDB; 58582; -. [Q08211-1] DR ProteomicsDB; 58583; -. [Q08211-2] DR Pumba; Q08211; -. DR TopDownProteomics; Q08211-1; -. [Q08211-1] DR Antibodypedia; 3194; 314 antibodies from 33 providers. DR DNASU; 1660; -. DR Ensembl; ENST00000367549.4; ENSP00000356520.3; ENSG00000135829.17. [Q08211-1] DR GeneID; 1660; -. DR KEGG; hsa:1660; -. DR MANE-Select; ENST00000367549.4; ENSP00000356520.3; NM_001357.5; NP_001348.2. DR UCSC; uc001gpr.4; human. [Q08211-1] DR AGR; HGNC:2750; -. DR CTD; 1660; -. DR DisGeNET; 1660; -. DR GeneCards; DHX9; -. DR HGNC; HGNC:2750; DHX9. DR HPA; ENSG00000135829; Low tissue specificity. DR MIM; 603115; gene. DR neXtProt; NX_Q08211; -. DR OpenTargets; ENSG00000135829; -. DR PharmGKB; PA27232; -. DR VEuPathDB; HostDB:ENSG00000135829; -. DR eggNOG; KOG0921; Eukaryota. DR GeneTree; ENSGT00940000155924; -. DR HOGENOM; CLU_001832_1_2_1; -. DR InParanoid; Q08211; -. DR OMA; RFKCELR; -. DR OrthoDB; 1095660at2759; -. DR PhylomeDB; Q08211; -. DR TreeFam; TF313601; -. DR BRENDA; 3.6.4.13; 2681. DR PathwayCommons; Q08211; -. DR Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1. DR Reactome; R-HSA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-9833482; PKR-mediated signaling. DR SignaLink; Q08211; -. DR SIGNOR; Q08211; -. DR BioGRID-ORCS; 1660; 748 hits in 1175 CRISPR screens. DR ChiTaRS; DHX9; human. DR GeneWiki; RNA_Helicase_A; -. DR GenomeRNAi; 1660; -. DR Pharos; Q08211; Tbio. DR PRO; PR:Q08211; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q08211; Protein. DR Bgee; ENSG00000135829; Expressed in ventricular zone and 213 other cell types or tissues. DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:ComplexPortal. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB. DR GO; GO:0097165; C:nuclear stress granule; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005726; C:perichromatin fibrils; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB. DR GO; GO:0016442; C:RISC complex; IDA:UniProtKB. DR GO; GO:0070578; C:RISC-loading complex; IMP:UniProtKB. DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:UniProtKB. DR GO; GO:0033679; F:3'-5' DNA/RNA helicase activity; IDA:UniProtKB. DR GO; GO:0034458; F:3'-5' RNA helicase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:UniProtKB. DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB. DR GO; GO:0003678; F:DNA helicase activity; IMP:UniProtKB. DR GO; GO:0003688; F:DNA replication origin binding; IDA:UniProtKB. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB. DR GO; GO:0061676; F:importin-alpha family protein binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB. DR GO; GO:0047429; F:nucleoside triphosphate diphosphatase activity; IDA:UniProtKB. DR GO; GO:1905538; F:polysome binding; IDA:UniProtKB. DR GO; GO:1990841; F:promoter-specific chromatin binding; IMP:UniProtKB. DR GO; GO:0001069; F:regulatory region RNA binding; IDA:UniProtKB. DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; ISS:UniProtKB. DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB. DR GO; GO:1905172; F:RISC complex binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB. DR GO; GO:0070063; F:RNA polymerase binding; IDA:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0035613; F:RNA stem-loop binding; IDA:UniProtKB. DR GO; GO:1990825; F:sequence-specific mRNA binding; IDA:UniProtKB. DR GO; GO:1990518; F:single-stranded 3'-5' DNA helicase activity; IDA:UniProtKB. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB. DR GO; GO:0035197; F:siRNA binding; IDA:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB. DR GO; GO:0003712; F:transcription coregulator activity; IMP:UniProtKB. DR GO; GO:0045142; F:triplex DNA binding; IDA:UniProtKB. DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:UniProtKB. DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IMP:UniProtKB. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:UniProtKB. DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IDA:ComplexPortal. DR GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-KW. DR GO; GO:0039695; P:DNA-templated viral transcription; IDA:UniProtKB. DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IDA: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:0035195; P:miRNA-mediated post-transcriptional gene silencing; IMP:UniProtKB. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:ComplexPortal. DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB. DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IDA:ComplexPortal. DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB. DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:UniProtKB. DR GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; IMP:UniProtKB. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:UniProtKB. DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB. DR GO; GO:0045089; P:positive regulation of innate immune response; ISS:UniProtKB. DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IMP:UniProtKB. DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB. DR GO; GO:0032741; P:positive regulation of interleukin-18 production; ISS:UniProtKB. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB. DR GO; GO:0060760; P:positive regulation of response to cytokine stimulus; IMP:UniProtKB. DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:UniProtKB. DR GO; GO:0050434; P:positive regulation of viral transcription; IDA:UniProtKB. DR GO; GO:1904973; P:positive regulation of viral translation; IMP:UniProtKB. DR GO; GO:1903608; P:protein localization to cytoplasmic stress granule; IMP:AgBase. DR GO; GO:0065003; P:protein-containing complex assembly; IDA:GO_Central. DR GO; GO:0070269; P:pyroptosis; ISS:UniProtKB. DR GO; GO:2000765; P:regulation of cytoplasmic translation; IDA:UniProtKB. DR GO; GO:0050691; P:regulation of defense response to virus by host; ISS:UniProtKB. DR GO; GO:0050684; P:regulation of mRNA processing; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0070922; P:RISC complex assembly; IMP:UniProtKB. DR GO; GO:0010501; P:RNA secondary structure unwinding; IDA:UniProtKB. DR CDD; cd17972; DEXHc_DHX9; 1. DR CDD; cd19854; DSRM_DHX9_rpt1; 1. DR CDD; cd19855; DSRM_DHX9_rpt2; 1. DR CDD; cd18791; SF2_C_RHA; 1. DR Gene3D; 1.20.120.1080; -; 1. DR Gene3D; 3.30.160.20; -; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR011709; DEAD-box_helicase_OB_fold. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR044447; DHX9_DEXHc. DR InterPro; IPR044445; DHX9_DSRM_1. DR InterPro; IPR044446; DHX9_DSRM_2. DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR048333; HA2_WH. DR InterPro; IPR007502; Helicase-assoc_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1. DR PANTHER; PTHR18934:SF119; ATP-DEPENDENT RNA HELICASE A; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00035; dsrm; 2. DR Pfam; PF21010; HA2_C; 1. DR Pfam; PF04408; HA2_N; 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; SSF54768; dsRNA-binding domain-like; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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. DR SWISS-2DPAGE; Q08211; -. DR Genevisible; Q08211; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; ATP-binding; KW Biological rhythms; Cytoplasm; Cytoskeleton; Direct protein sequencing; KW DNA replication; DNA-binding; Helicase; Host-virus interaction; Hydrolase; KW Immunity; Inflammatory response; Innate immunity; Isopeptide bond; KW Manganese; 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..1270 FT /note="ATP-dependent RNA helicase A" FT /id="PRO_0000055157" FT DOMAIN 3..71 FT /note="DRBM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266, FT ECO:0000269|PubMed:23361462, ECO:0000269|PubMed:9111062" FT DOMAIN 180..252 FT /note="DRBM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266, FT ECO:0000269|PubMed:23361462, ECO:0000269|PubMed:9111062" FT DOMAIN 398..564 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541, FT ECO:0000269|PubMed:20510246" FT DOMAIN 636..809 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 1..250 FT /note="Interaction with CREBBP" FT /evidence="ECO:0000269|PubMed:9323138" FT REGION 5..9 FT /note="siRNA-binding" FT /evidence="ECO:0000269|PubMed:23361462, FT ECO:0007744|PDB:3VYY" FT REGION 53..55 FT /note="siRNA-binding" FT /evidence="ECO:0000269|PubMed:23361462, FT ECO:0007744|PDB:3VYY" FT REGION 83..118 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 182..186 FT /note="siRNA-binding" FT /evidence="ECO:0000269|PubMed:23361462, FT ECO:0007744|PDB:3VYX" FT REGION 230..325 FT /note="Interaction with BRCA1" FT /evidence="ECO:0000269|PubMed:9662397" FT REGION 234..236 FT /note="siRNA-binding" FT /evidence="ECO:0000305|PubMed:23361462" FT REGION 255..664 FT /note="Necessary for interaction with RNA polymerase II FT holoenzyme" FT /evidence="ECO:0000269|PubMed:9323138" FT REGION 313..952 FT /note="Necessary for interaction with H2AX" FT /evidence="ECO:0000269|PubMed:15613478" FT REGION 331..380 FT /note="MTAD" FT /evidence="ECO:0000269|PubMed:11416126" FT REGION 398..809 FT /note="Core helicase" FT /evidence="ECO:0000305|PubMed:25062910" FT REGION 588..608 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 831..919 FT /note="HA2" FT /evidence="ECO:0000269|PubMed:25062910" FT REGION 958..1074 FT /note="OB-fold" FT /evidence="ECO:0000269|PubMed:20696886, FT ECO:0000269|PubMed:25062910, ECO:0000269|PubMed:25149208" FT REGION 1150..1270 FT /note="RGG" FT /evidence="ECO:0000269|PubMed:10207077, FT ECO:0000269|PubMed:25062910, ECO:0000269|PubMed:25149208, FT ECO:0000269|PubMed:9111062" FT REGION 1229..1248 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 511..514 FT /note="DEIH box" FT MOTIF 586..595 FT /note="Nuclear localization signal (NLS1)" FT /evidence="ECO:0000255" FT MOTIF 1155..1173 FT /note="Nuclear localization signal (NLS2)" FT /evidence="ECO:0000269|PubMed:16375861" FT BINDING 411..419 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:11416126, FT ECO:0000269|PubMed:20510246, ECO:0007744|PDB:3LLM" FT BINDING 418 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:20510246, FT ECO:0007744|PDB:3LLM" FT BINDING 512 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:20510246, FT ECO:0007744|PDB:3LLM" FT MOD_RES 87 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569" FT MOD_RES 125 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 146 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:O70133" FT MOD_RES 146 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 191 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 199 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 321 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 449 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 506 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1024 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1166 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:O70133" FT MOD_RES 1175 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1219 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:O70133" FT MOD_RES 1235 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:O70133" FT MOD_RES 1242 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:O70133" FT MOD_RES 1249 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:O70133" FT MOD_RES 1265 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:O70133" FT CROSSLNK 697 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..1035 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:19054851, FT ECO:0000303|PubMed:8690889" FT /id="VSP_042314" FT VARIANT 894 FT /note="I -> V (in dbSNP:rs1049264)" FT /evidence="ECO:0000269|PubMed:8344961" FT /id="VAR_052179" FT MUTAGEN 5 FT /note="K->A: Reduces siRNA-binding and interaction with FT AGO2; when associated with A-6." FT /evidence="ECO:0000269|PubMed:23361462" FT MUTAGEN 6 FT /note="N->A: Reduces siRNA-binding; when associated with FT A-5." FT /evidence="ECO:0000269|PubMed:23361462" FT MUTAGEN 9 FT /note="Y->A: Inhibits siRNA-binding and interaction with FT AGO2." FT /evidence="ECO:0000269|PubMed:23361462" FT MUTAGEN 30 FT /note="N->A: Does not reduce siRNA-binding and interaction FT with AGO2." FT /evidence="ECO:0000269|PubMed:23361462" FT MUTAGEN 53 FT /note="N->A: Inhibits siRNA-binding and decreases FT interaction with AGO2; when associated with A-54 and A-55." FT /evidence="ECO:0000269|PubMed:23361462" FT MUTAGEN 54 FT /note="K->A: Inhibits siRNA-binding and decreases FT interaction with AGO2; when associated with A-53 and A-55." FT /evidence="ECO:0000269|PubMed:23361462" FT MUTAGEN 55 FT /note="K->A: Inhibits siRNA-binding and decreases FT interaction with AGO2; when associated with A-53 and A-54." FT /evidence="ECO:0000269|PubMed:23361462" FT MUTAGEN 182 FT /note="K->A: Reduces siRNA-binding and interaction with FT AGO2." FT /evidence="ECO:0000269|PubMed:23361462" FT MUTAGEN 186 FT /note="N->A: Reduces siRNA-binding and interaction with FT AGO2; when associated with A-187." FT /evidence="ECO:0000269|PubMed:23361462" FT MUTAGEN 187 FT /note="Q->A: Reduces siRNA-binding and interaction with FT AGO2; when associated with A-186." FT /evidence="ECO:0000269|PubMed:23361462" FT MUTAGEN 207 FT /note="H->A: Reduces siRNA-binding and interaction with FT AGO2." FT /evidence="ECO:0000269|PubMed:23361462" FT MUTAGEN 234 FT /note="N->A: Inhibits siRNA-binding and interaction with FT AGO2; when associated with A-235 and A-236." FT /evidence="ECO:0000269|PubMed:23361462" FT MUTAGEN 235 FT /note="K->A: Inhibits siRNA-binding and interaction with FT AGO2; when associated with A-234 and A-236." FT /evidence="ECO:0000269|PubMed:23361462" FT MUTAGEN 236 FT /note="K->A: Inhibits siRNA-binding and interaction with FT AGO2; when associated with A-234 and A-235." FT /evidence="ECO:0000269|PubMed:23361462" FT MUTAGEN 332 FT /note="W->A: Abrogates transcriptional activation by the FT MTAD region. No change in RNA polymerase II holoenzyme FT binding." FT /evidence="ECO:0000269|PubMed:11416126" FT MUTAGEN 339 FT /note="W->A: Abrogates transcriptional activation and RNA FT polymerase II binding by the MTAD region. No change in ATP FT binding and ATPase activities." FT /evidence="ECO:0000269|PubMed:11416126" FT MUTAGEN 342 FT /note="W->A: Abrogates transcriptional activation by the FT MTAD region. No change in RNA polymerase II holoenzyme FT binding." FT /evidence="ECO:0000269|PubMed:11416126" FT MUTAGEN 347 FT /note="I->A: Reduces NUP98-induced mRNA transcription and FT alternative splicing activities." FT /evidence="ECO:0000269|PubMed:28221134" FT MUTAGEN 417 FT /note="K->R,N: Inhibits interaction with AGO2, DICER1 and FT TARBP2. Abrogates helicase activity and transcriptional FT activation. Does not inhibit binding to origins of DNA FT replication." FT /evidence="ECO:0000269|PubMed:15355351, FT ECO:0000269|PubMed:17531811, ECO:0000269|PubMed:24990949, FT ECO:0000269|PubMed:9323138" FT MUTAGEN 417 FT /note="K->R: Reduces NUP98-induced mRNA transcription and FT alternative splicing activities." FT /evidence="ECO:0000269|PubMed:28221134" FT MUTAGEN 511 FT /note="D->A: Does not inhibit binding to origins of DNA FT replication; when associated with A-512." FT /evidence="ECO:0000269|PubMed:24990949" FT MUTAGEN 512 FT /note="E->A: Does not inhibit binding to origins of DNA FT replication; when associated with A-511." FT /evidence="ECO:0000269|PubMed:24990949" FT MUTAGEN 543 FT /note="S->L: Does not inhibit binding to origins of DNA FT replication." FT /evidence="ECO:0000269|PubMed:24990949" FT MUTAGEN 1160 FT /note="R->A: Localizes in the nucleus and interacts with FT the importin complex." FT /evidence="ECO:0000269|PubMed:16375861" FT MUTAGEN 1163 FT /note="K->A: Localizes in the cytoplasm and does not FT interact with the importin complex." FT /evidence="ECO:0000269|PubMed:16375861" FT MUTAGEN 1163 FT /note="Missing: Abolishes nuclear localization." FT /evidence="ECO:0000269|PubMed:10207077" FT MUTAGEN 1166 FT /note="R->A: Localizes in the nucleus and the cytoplasm and FT interacts weakly with the importin complex." FT /evidence="ECO:0000269|PubMed:16375861" FT MUTAGEN 1166 FT /note="R->L: Abolishes nuclear localization." FT /evidence="ECO:0000269|PubMed:10207077" FT MUTAGEN 1166 FT /note="Missing: Abolishes nuclear localization." FT /evidence="ECO:0000269|PubMed:10207077" FT CONFLICT 20 FT /note="S -> T (in Ref. 1; AAB48855)" FT /evidence="ECO:0000305" FT CONFLICT 108..109 FT /note="TM -> HH (in Ref. 1; AAB48855)" FT /evidence="ECO:0000305" FT CONFLICT 114..116 FT /note="PPH -> LHI (in Ref. 1; AAB48855)" FT /evidence="ECO:0000305" FT CONFLICT 186 FT /note="N -> I (in Ref. 1; AAB48855)" FT /evidence="ECO:0000305" FT CONFLICT 260 FT /note="S -> T (in Ref. 1; AAB48855)" FT /evidence="ECO:0000305" FT CONFLICT 478 FT /note="I -> V (in Ref. 1; AAB48855)" FT /evidence="ECO:0000305" FT CONFLICT 521 FT /note="D -> S (in Ref. 1; AAB48855)" FT /evidence="ECO:0000305" FT CONFLICT 541 FT /note="L -> F (in Ref. 1; AAB48855)" FT /evidence="ECO:0000305" FT CONFLICT 560..565 FT /note="IIEVYG -> SLKLW (in Ref. 1; AAB48855)" FT /evidence="ECO:0000305" FT CONFLICT 590 FT /note="D -> K (in Ref. 5; AAH25245)" FT /evidence="ECO:0000305" FT CONFLICT 749 FT /note="A -> S (in Ref. 1; AAB48855 and 3; CAA71668)" FT /evidence="ECO:0000305" FT CONFLICT 768..770 FT /note="VRP -> STA (in Ref. 1; AAB48855 and 3; CAA71668)" FT /evidence="ECO:0000305" FT CONFLICT 828 FT /note="A -> G (in Ref. 5; AAI07882)" FT /evidence="ECO:0000305" FT CONFLICT 899 FT /note="R -> Q (in Ref. 1; AAB48855)" FT /evidence="ECO:0000305" FT CONFLICT 1037 FT /note="K -> N (in Ref. 1; AAB48855)" FT /evidence="ECO:0000305" FT CONFLICT 1063 FT /note="T -> P (in Ref. 1; AAB48855 and 3; CAA71668)" FT /evidence="ECO:0000305" FT CONFLICT 1140 FT /note="R -> E (in Ref. 1; AAB48855)" FT /evidence="ECO:0000305" FT CONFLICT 1204..1211 FT /note="NSFRAGYG -> TPSGRIC (in Ref. 1; AAB48855)" FT /evidence="ECO:0000305" FT CONFLICT 1261..1270 FT /note="FGQGRGGGGY -> LDIEEEVAAIKLGYVSSVCRQ (in Ref. 1; FT AAB48855)" FT /evidence="ECO:0000305" FT HELIX 4..14 FT /evidence="ECO:0007829|PDB:3VYY" FT STRAND 20..28 FT /evidence="ECO:0007829|PDB:3VYY" FT STRAND 31..39 FT /evidence="ECO:0007829|PDB:3VYY" FT STRAND 47..53 FT /evidence="ECO:0007829|PDB:3VYY" FT HELIX 54..71 FT /evidence="ECO:0007829|PDB:3VYY" FT HELIX 77..79 FT /evidence="ECO:0007829|PDB:3VYY" FT HELIX 170..173 FT /evidence="ECO:0007829|PDB:3VYX" FT TURN 178..180 FT /evidence="ECO:0007829|PDB:3VYX" FT HELIX 181..191 FT /evidence="ECO:0007829|PDB:3VYX" FT STRAND 199..204 FT /evidence="ECO:0007829|PDB:3VYX" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:3VYX" FT STRAND 210..218 FT /evidence="ECO:0007829|PDB:3VYX" FT HELIX 220..222 FT /evidence="ECO:0007829|PDB:3VYX" FT STRAND 223..234 FT /evidence="ECO:0007829|PDB:3VYX" FT HELIX 235..252 FT /evidence="ECO:0007829|PDB:3VYX" FT HELIX 280..293 FT /evidence="ECO:0007829|PDB:8SZP" FT TURN 341..344 FT /evidence="ECO:0007829|PDB:8SZP" FT TURN 351..354 FT /evidence="ECO:0007829|PDB:3LLM" FT HELIX 357..374 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 376..385 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 389..393 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 394..403 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 405..411 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 417..431 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 435..437 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 439..446 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 447..460 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 467..473 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 476..478 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 482..490 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 491..497 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 502..504 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 506..510 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 513..515 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 518..533 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 537..543 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 549..554 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 560..563 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 570..573 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 575..582 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 618..624 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 634..645 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 652..656 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 659..671 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 674..676 FT /evidence="ECO:0007829|PDB:8SZP" FT TURN 678..680 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 681..687 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 692..695 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 696..698 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 707..712 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 715..718 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 723..730 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 733..736 FT /evidence="ECO:0007829|PDB:8SZP" FT TURN 742..744 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 748..752 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 755..762 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 763..765 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 767..775 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 779..783 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 792..794 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 799..807 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 813..817 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 820..822 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 826..838 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 850..857 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 858..860 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 862..873 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 877..887 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 896..899 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 902..908 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 914..928 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 929..931 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 933..942 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 947..967 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 971..974 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 981..983 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 986..999 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 1003..1008 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 1011..1013 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 1019..1022 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 1026..1028 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 1041..1044 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 1046..1058 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 1064..1070 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 1075..1077 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 1079..1084 FT /evidence="ECO:0007829|PDB:8SZP" FT TURN 1085..1087 FT /evidence="ECO:0007829|PDB:8SZP" FT STRAND 1088..1091 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 1094..1116 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 1118..1123 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 1126..1139 FT /evidence="ECO:0007829|PDB:8SZP" FT HELIX 1142..1144 FT /evidence="ECO:0007829|PDB:8SZP" SQ SEQUENCE 1270 AA; 140958 MW; A607DA8F4C4B217A CRC64; MGDVKNFLYA WCGKRKMTPS YEIRAVGNKN RQKFMCEVQV EGYNYTGMGN STNKKDAQSN AARDFVNYLV RINEIKSEEV PAFGVASPPP LTDTPDTTAN AEGDLPTTMG GPLPPHLALK AENNSEVGAS GYGVPGPTWD RGANLKDYYS RKEEQEVQAT LESEEVDLNA GLHGNWTLEN AKARLNQYFQ KEKIQGEYKY TQVGPDHNRS FIAEMTIYIK QLGRRIFARE HGSNKKLAAQ SCALSLVRQL YHLGVVEAYS GLTKKKEGET VEPYKVNLSQ DLEHQLQNII QELNLEILPP PEDPSVPVAL NIGKLAQFEP SQRQNQVGVV PWSPPQSNWN PWTSSNIDEG PLAFATPEQI SMDLKNELMY QLEQDHDLQA ILQERELLPV KKFESEILEA ISQNSVVIIR GATGCGKTTQ VPQFILDDFI QNDRAAECNI VVTQPRRISA VSVAERVAFE RGEEPGKSCG YSVRFESILP RPHASIMFCT VGVLLRKLEA GIRGISHVIV DEIHERDINT DFLLVVLRDV VQAYPEVRIV LMSATIDTSM FCEYFFNCPI IEVYGRTYPV QEYFLEDCIQ MTHFVPPPKD KKKKDKDDDG GEDDDANCNL ICGDEYGPET RLSMSQLNEK ETPFELIEAL LKYIETLNVP GAVLVFLPGW NLIYTMQKHL EMNPHFGSHR YQILPLHSQI PREEQRKVFD PVPVGVTKVI LSTNIAETSI TINDVVYVID SCKQKVKLFT AHNNMTNYAT VWASKTNLEQ RKGRAGRVRP GFCFHLCSRA RFERLETHMT PEMFRTPLHE IALSIKLLRL GGIGQFLAKA IEPPPLDAVI EAEHTLRELD ALDANDELTP LGRILAKLPI EPRFGKMMIM GCIFYVGDAI CTIAAATCFP EPFINEGKRL GYIHRNFAGN RFSDHVALLS VFQAWDDARM GGEEAEIRFC EHKRLNMATL RMTWEAKVQL KEILINSGFP EDCLLTQVFT NTGPDNNLDV VISLLAFGVY PNVCYHKEKR KILTTEGRNA LIHKSSVNCP FSSQDMKYPS PFFVFGEKIR TRAISAKGMT LVTPLQLLLF ASKKVQSDGQ IVLVDDWIKL QISHEAAACI TGLRAAMEAL VVEVTKQPAI ISQLDPVNER MLNMIRQISR PSAAGINLMI GSTRYGDGPR PPKMARYDNG SGYRRGGSSY SGGGYGGGYS SGGYGSGGYG GSANSFRAGY GAGVGGGYRG VSRGGFRGNS GGDYRGPSGG YRGSGGFQRG GGRGAYGTGY FGQGRGGGGY //