DHX9_HUMAN
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 03-AUG-2022, entry version 230.
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- 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 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 [69]
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 -!- 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="http://atlasgeneticsoncology.org/Genes/DHX9ID44879ch1q25.html";
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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 PDBsum; 3LLM; -.
DR PDBsum; 3VYX; -.
DR PDBsum; 3VYY; -.
DR AlphaFoldDB; Q08211; -.
DR BMRB; Q08211; -.
DR SMR; Q08211; -.
DR BioGRID; 108025; 439.
DR ComplexPortal; CPX-1080; CRD-mediated mRNA stability complex.
DR CORUM; Q08211; -.
DR DIP; DIP-31504N; -.
DR IntAct; Q08211; 141.
DR MINT; Q08211; -.
DR STRING; 9606.ENSP00000356520; -.
DR GlyGen; Q08211; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q08211; -.
DR MetOSite; Q08211; -.
DR PhosphoSitePlus; Q08211; -.
DR SwissPalm; Q08211; -.
DR BioMuta; DHX9; -.
DR DMDM; 116241330; -.
DR SWISS-2DPAGE; Q08211; -.
DR CPTAC; CPTAC-355; -.
DR CPTAC; CPTAC-356; -.
DR EPD; Q08211; -.
DR jPOST; Q08211; -.
DR MassIVE; Q08211; -.
DR MaxQB; Q08211; -.
DR PaxDb; Q08211; -.
DR PeptideAtlas; Q08211; -.
DR PRIDE; Q08211; -.
DR ProteomicsDB; 58582; -. [Q08211-1]
DR ProteomicsDB; 58583; -. [Q08211-2]
DR TopDownProteomics; Q08211-1; -. [Q08211-1]
DR Antibodypedia; 3194; 283 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 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; YGPETRM; -.
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 SignaLink; Q08211; -.
DR SIGNOR; Q08211; -.
DR BioGRID-ORCS; 1660; 709 hits in 1093 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 211 other tissues.
DR Genevisible; Q08211; HS.
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:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005726; C:perichromatin fibrils; IDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0005844; C:polysome; 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:0017111; F:nucleoside-triphosphatase activity; ISS: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: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:0098795; P:global gene silencing by mRNA cleavage; IMP: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: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:2000637; P:positive regulation of miRNA-mediated gene silencing; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:1905698; P:positive regulation of polysome binding; 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 Gene3D; 3.40.50.300; -; 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; 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; 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 A-
FT 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 TURN 341..344
FT /evidence="ECO:0007829|PDB:3LLM"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:3LLM"
FT HELIX 357..374
FT /evidence="ECO:0007829|PDB:3LLM"
FT HELIX 376..386
FT /evidence="ECO:0007829|PDB:3LLM"
FT HELIX 389..393
FT /evidence="ECO:0007829|PDB:3LLM"
FT HELIX 394..403
FT /evidence="ECO:0007829|PDB:3LLM"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:3LLM"
FT HELIX 417..431
FT /evidence="ECO:0007829|PDB:3LLM"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:3LLM"
FT STRAND 439..446
FT /evidence="ECO:0007829|PDB:3LLM"
FT HELIX 447..459
FT /evidence="ECO:0007829|PDB:3LLM"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:3LLM"
FT STRAND 467..473
FT /evidence="ECO:0007829|PDB:3LLM"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:3LLM"
FT STRAND 482..490
FT /evidence="ECO:0007829|PDB:3LLM"
FT HELIX 491..500
FT /evidence="ECO:0007829|PDB:3LLM"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:3LLM"
FT HELIX 518..533
FT /evidence="ECO:0007829|PDB:3LLM"
FT STRAND 537..543
FT /evidence="ECO:0007829|PDB:3LLM"
FT HELIX 549..554
FT /evidence="ECO:0007829|PDB:3LLM"
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
