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ATP-dependent RNA helicase A (EC 3.6.4.13) (DEAH box protein 9) (DExH-box helicase 9) (Leukophysin) (LKP) (Nuclear DNA helicase II) (NDH II) (RNA helicase A)

 DHX9_HUMAN              Reviewed;        1270 AA.
Q08211; B2RNV4; Q05CI5; Q12803; Q32Q22; Q5VY62; Q6PD69; Q99556;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 4.
25-OCT-2017, entry version 196.
RecName: Full=ATP-dependent RNA helicase A {ECO:0000305};
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};
AltName: Full=DEAH box protein 9;
AltName: Full=DExH-box helicase 9 {ECO:0000312|HGNC:HGNC:2750};
AltName: Full=Leukophysin {ECO:0000303|PubMed:8690889};
Short=LKP {ECO:0000303|PubMed:8690889};
AltName: Full=Nuclear DNA helicase II {ECO:0000303|PubMed:1537828, ECO:0000303|PubMed:8344961, ECO:0000303|PubMed:9111062};
Short=NDH II {ECO:0000303|PubMed:8344961, ECO:0000303|PubMed:9111062};
AltName: Full=RNA helicase A {ECO:0000303|PubMed:9111062};
Name=DHX9 {ECO:0000312|HGNC:HGNC:2750};
Synonyms=DDX9 {ECO:0000312|HGNC:HGNC:2750}, LKP, NDH2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
VARIANT VAL-894.
PubMed=8344961;
Lee C.-G., Hurwitz J.;
"Human RNA helicase A is homologous to the maleless protein of
Drosophila.";
J. Biol. Chem. 268:16822-16830(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
PubMed=8690889;
Abdelhaleem M.M., Hameed S., Klassen D., Greenberg A.H.;
"Leukophysin: an RNA helicase A-related molecule identified in
cytotoxic T cell granules and vesicles.";
J. Immunol. 156:2026-2035(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN DNA/RNA UNWINDING,
CATALYTIC ACTIVITY, DNA-BINDING, RNA-BINDING, AND DOMAIN DRBM.
PubMed=9111062; DOI=10.1074/jbc.272.17.11487;
Zhang S., Grosse F.;
"Domain structure of human nuclear DNA helicase II (RNA helicase A).";
J. Biol. Chem. 272:11487-11494(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, Muscle, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PARTIAL PROTEIN SEQUENCE, FUNCTION IN TRANSCRIPTIONAL REGULATION,
INTERACTION WITH SMN1; SMN COMPLEX AND RNA POLYMERASE II HOLOENZYME,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11149922; DOI=10.1083/jcb.152.1.75;
Pellizzoni L., Charroux B., Rappsilber J., Mann M., Dreyfuss G.;
"A functional interaction between the survival motor neuron complex
and RNA polymerase II.";
J. Cell Biol. 152:75-85(2001).
[9]
FUNCTION IN DNA/RNA UNWINDING, CATALYTIC ACTIVITY, AND RNA-BINDING.
PubMed=1537828;
Lee C.G., Hurwitz J.;
"A new RNA helicase isolated from HeLa cells that catalytically
translocates in the 3' to 5' direction.";
J. Biol. Chem. 267:4398-4407(1992).
[10]
FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH CREBBP AND
RNA POLYMERASE II HOLOENZYME, AND MUTAGENESIS OF LYS-417.
PubMed=9323138; DOI=10.1016/S0092-8674(00)80376-1;
Nakajima T., Uchida C., Anderson S.F., Lee C.-G., Hurwitz J.,
Parvin J.D., Montminy M.;
"RNA helicase A mediates association of CBP with RNA polymerase II.";
Cell 90:1107-1112(1997).
[11]
FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION, RNA-BINDING, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=9162007;
Tang H., Gaietta G.M., Fischer W.H., Ellisman M.H., Wong-Staal F.;
"A cellular cofactor for the constitutive transport element of type D
retrovirus.";
Science 276:1412-1415(1997).
[12]
FUNCTION IN TRANSCRIPTIONAL REGULATION, AND INTERACTION WITH BRCA1.
PubMed=9662397; DOI=10.1038/930;
Anderson S.F., Schlegel B.P., Nakajima T., Wolpin E.S., Parvin J.D.;
"BRCA1 protein is linked to the RNA polymerase II holoenzyme complex
via RNA helicase A.";
Nat. Genet. 19:254-256(1998).
[13]
SUBCELLULAR LOCATION, RNA-BINDING, AND DNA-BINDING.
PubMed=10198287;
Zhang S., Herrmann C., Grosse F.;
"Pre-mRNA and mRNA binding of human nuclear DNA helicase II (RNA
helicase A).";
J. Cell Sci. 112:1055-1064(1999).
[14]
SUBCELLULAR LOCATION, DOMAIN RGG, AND MUTAGENESIS OF LYS-1163 AND
ARG-1166.
PubMed=10207077; DOI=10.1128/MCB.19.5.3540;
Tang H., McDonald D., Middlesworth T., Hope T.J., Wong-Staal F.;
"The carboxyl terminus of RNA helicase A contains a bidirectional
nuclear transport domain.";
Mol. Cell. Biol. 19:3540-3550(1999).
[15]
FUNCTION (MICROBIAL INFECTION), AND RNA-BINDING (MICROBIAL INFECTION).
PubMed=9892698;
Li J., Tang H., Mullen T.M., Westberg C., Reddy T.R., Rose D.W.,
Wong-Staal F.;
"A role for RNA helicase A in post-transcriptional regulation of HIV
type 1.";
Proc. Natl. Acad. Sci. U.S.A. 96:709-714(1999).
[16]
FUNCTION IN MRNA EXPORT, AND INTERACTION WITH NXF1.
PubMed=10924507; DOI=10.1074/jbc.M003933200;
Tang H., Wong-Staal F.;
"Specific interaction between RNA helicase A and Tap, two cellular
proteins that bind to the constitutive transport element of type D
retrovirus.";
J. Biol. Chem. 275:32694-32700(2000).
[17]
FUNCTION IN TRANSCRIPTIONAL REGULATION, PROMOTER DNA-BINDING, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11038348; DOI=10.1074/jbc.M004481200;
Myoehaenen S., Baylin S.B.;
"Sequence-specific DNA binding activity of RNA helicase A to the
p16INK4a promoter.";
J. Biol. Chem. 276:1634-1642(2001).
[18]
FUNCTION (MICROBIAL INFECTION), AND RNA-BINDING (MICROBIAL INFECTION).
PubMed=11096080; DOI=10.1074/jbc.M006892200;
Fujii R., Okamoto M., Aratani S., Oishi T., Ohshima T., Taira K.,
Baba M., Fukamizu A., Nakajima T.;
"A role of RNA helicase A in cis-acting transactivation response
element-mediated transcriptional regulation of human immunodeficiency
virus type 1.";
J. Biol. Chem. 276:5445-5451(2001).
[19]
FUNCTION IN MRNA EXPORT, RNA-BINDING, AND INTERACTION WITH AKAP8L.
PubMed=11402034; DOI=10.1074/jbc.M102809200;
Yang J.P., Tang H., Reddy T.R., Wong-Staal F.;
"Mapping the functional domains of HAP95, a protein that binds RNA
helicase A and activates the constitutive transport element of type D
retroviruses.";
J. Biol. Chem. 276:30694-30700(2001).
[20]
FUNCTION IN TRANSCRIPTIONAL REGULATION, CATALYTIC ACTIVITY,
INTERACTION WITH RNA POLYMERASE II HOLOENZYME, ATP-BINDING, DOMAIN
MTAD, AND MUTAGENESIS OF TRP-332; TRP-339 AND TRP-342.
PubMed=11416126; DOI=10.1128/MCB.21.14.4460-4469.2001;
Aratani S., Fujii R., Oishi T., Fujita H., Amano T., Ohshima T.,
Hagiwara M., Fukamizu A., Nakajima T.;
"Dual roles of RNA helicase A in CREB-dependent transcription.";
Mol. Cell. Biol. 21:4460-4469(2001).
[21]
FUNCTION, INTERACTION WITH ACTB AND HNRNPC, AND SUBCELLULAR LOCATION.
PubMed=11687588; DOI=10.1074/jbc.M109393200;
Zhang S., Buder K., Burkhardt C., Schlott B., Goerlach M., Grosse F.;
"Nuclear DNA helicase II/RNA helicase A binds to filamentous actin.";
J. Biol. Chem. 277:843-853(2002).
[22]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[23]
INTERACTION WITH ILF3.
PubMed=12946349;
Reichman T.W., Parrott A.M., Fierro-Monti I., Caron D.J., Kao P.N.,
Lee C.G., Li H., Mathews M.B.;
"Selective regulation of gene expression by nuclear factor 110, a
member of the NF90 family of double-stranded RNA-binding proteins.";
J. Mol. Biol. 332:85-98(2003).
[24]
FUNCTION IN TRANSCRIPTIONAL REGULATION, AND INTERACTION WITH MBD2.
PubMed=12665568; DOI=10.1128/MCB.23.8.2645-2657.2003;
Fujita H., Fujii R., Aratani S., Amano T., Fukamizu A., Nakajima T.;
"Antithetic effects of MBD2a on gene regulation.";
Mol. Cell. Biol. 23:2645-2657(2003).
[25]
FUNCTION IN DNA/RNA UNWINDING, INTERACTION WITH TOP2A, AND
DOUBLE-STRAND DNA- AND RNA-BINDING.
PubMed=12711669; DOI=10.1093/nar/gkg328;
Zhou K., Choe K.-T., Zaidi Z., Wang Q., Mathews M.B., Lee C.-G.;
"RNA helicase A interacts with dsDNA and topoisomerase IIalpha.";
Nucleic Acids Res. 31:2253-2260(2003).
[26]
FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH RELA, AND
MUTAGENESIS OF LYS-417.
PubMed=15355351; DOI=10.1111/j.1432-1033.2004.04314.x;
Tetsuka T., Uranishi H., Sanda T., Asamitsu K., Yang J.-P.,
Wong-Staal F., Okamoto T.;
"RNA helicase A interacts with nuclear factor kappaB p65 and functions
as a transcriptional coactivator.";
Eur. J. Biochem. 271:3741-3751(2004).
[27]
METHYLATION, INTERACTION WITH PRMT1, AND DOMAIN RGG.
PubMed=15084609; DOI=10.1074/jbc.C300512200;
Smith W.A., Schurter B.T., Wong-Staal F., David M.;
"Arginine methylation of RNA helicase a determines its subcellular
localization.";
J. Biol. Chem. 279:22795-22798(2004).
[28]
INTERACTION WITH XRCC5, AND PHOSPHORYLATION BY PRKDC.
PubMed=14704337; DOI=10.1093/nar/gkg933;
Zhang S., Schlott B., Goerlach M., Grosse F.;
"DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA
helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent
manner.";
Nucleic Acids Res. 32:1-10(2004).
[29]
INTERACTION WITH H2AFX.
PubMed=15613478; DOI=10.1074/jbc.M411444200;
Mischo H.E., Hemmerich P., Grosse F., Zhang S.;
"Actinomycin D induces histone gamma-H2AX foci and complex formation
of gamma-H2AX with Ku70 and nuclear DNA helicase II.";
J. Biol. Chem. 280:9586-9594(2005).
[30]
INTERACTION WITH WRN.
PubMed=15995249; DOI=10.1074/jbc.M503882200;
Friedemann J., Grosse F., Zhang S.;
"Nuclear DNA helicase II (RNA helicase A) interacts with Werner
syndrome helicase and stimulates its exonuclease activity.";
J. Biol. Chem. 280:31303-31313(2005).
[31]
SUBCELLULAR LOCATION, INTERACTION WITH THE IMPORTIN COMPLEX, NUCLEAR
LOCALIZATION SIGNAL, AND MUTAGENESIS OF ARG-1160; LYS-1163 AND
ARG-1166.
PubMed=16375861; DOI=10.1016/j.bbrc.2005.11.161;
Aratani S., Oishi T., Fuj ita H., Nakazawa M., Fujii R., Imamoto N.,
Yoneda Y., Fukamizu A., Nakajima T.;
"The nuclear import of RNA helicase A is mediated by importin-
alpha3.";
Biochem. Biophys. Res. Commun. 340:125-133(2006).
[32]
FUNCTION IN VIRAL MRNA TRANSLATION (MICROBIAL INFECTION), FUNCTION IN
MRNA TRANSLATION, ASSOCIATION WITH POLYRIBOSOMES, RNA-BINDING
(MICROBIAL INFECTION), RNA-BINDING, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16680162; DOI=10.1038/nsmb1092;
Hartman T.R., Qian S., Bolinger C., Fernandez S., Schoenberg D.R.,
Boris-Lawrie K.;
"RNA helicase A is necessary for translation of selected messenger
RNAs.";
Nat. Struct. Mol. Biol. 13:509-516(2006).
[33]
INTERACTION WITH SP7, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=17303075; DOI=10.1016/j.bbrc.2007.01.150;
Amorim B.R., Okamura H., Yoshida K., Qiu L., Morimoto H., Haneji T.;
"The transcriptional factor Osterix directly interacts with RNA
helicase A.";
Biochem. Biophys. Res. Commun. 355:347-351(2007).
[34]
INTERACTION WITH H2AFX, AND SUBCELLULAR LOCATION.
PubMed=17498979; DOI=10.1016/j.cellbi.2007.03.027;
Zhang S., Hemmerich P., Grosse F.;
"Werner syndrome helicase (WRN), nuclear DNA helicase II (NDH II) and
histone gammaH2AX are localized to the centrosome.";
Cell Biol. Int. 31:1109-1121(2007).
[35]
INTERACTION WITH ZIC2.
PubMed=17251188; DOI=10.1074/jbc.M610821200;
Ishiguro A., Ideta M., Mikoshiba K., Chen D.J., Aruga J.;
"ZIC2-dependent transcriptional regulation is mediated by DNA-
dependent protein kinase, poly(ADP-ribose) polymerase, and RNA
helicase A.";
J. Biol. Chem. 282:9983-9995(2007).
[36]
FUNCTION IN RISC LOADING COMPLEX, ASSOCIATION WITH THE RISC LOADING
COMPLEX, INTERACTION WITH AGO2; DICER1 AND TARBP2, AND MUTAGENESIS OF
LYS-417.
PubMed=17531811; DOI=10.1016/j.molcel.2007.04.016;
Robb G.B., Rana T.M.;
"RNA helicase A interacts with RISC in human cells and functions in
RISC loading.";
Mol. Cell 26:523-537(2007).
[37]
IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1,
AND SUBCELLULAR LOCATION.
PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[40]
FUNCTION, FUNCTION (MICROBIAL INFECTION), INTERACTION WITH EIF2AK2,
AND PHOSPHORYLATION BY EIF2AK2.
PubMed=19229320; DOI=10.1371/journal.ppat.1000311;
Sadler A.J., Latchoumanin O., Hawkes D., Mak J., Williams B.R.;
"An antiviral response directed by PKR phosphorylation of the RNA
helicase A.";
PLoS Pathog. 5:E1000311-E1000311(2009).
[41]
FUNCTION IN MRNA STABILITY, COMPONENT OF THE CRD-MEDIATED MRNA
STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR
LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19029303; DOI=10.1261/rna.1175909;
Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M.,
Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.;
"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic
RNPs.";
RNA 15:104-115(2009).
[42]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191; LYS-199 AND LYS-1024,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[43]
FUNCTION AS A TRIPLEX DNA HELICASE, FUNCTION IN DNA REPLICATION, AND
CATALYTIC ACTIVITY.
PubMed=20669935; DOI=10.1021/bi100795m;
Jain A., Bacolla A., Chakraborty P., Grosse F., Vasquez K.M.;
"Human DHX9 helicase unwinds triple-helical DNA structures.";
Biochemistry 49:6992-6999(2010).
[44]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH MYD88, MICROBIAL
DNA-BINDING (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20696886; DOI=10.1073/pnas.1006539107;
Kim T., Pazhoor S., Bao M., Zhang Z., Hanabuchi S., Facchinetti V.,
Bover L., Plumas J., Chaperot L., Qin J., Liu Y.J.;
"Aspartate-glutamate-alanine-histidine box motif (DEAH)/RNA helicase A
helicases sense microbial DNA in human plasmacytoid dendritic cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:15181-15186(2010).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[46]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[47]
FUNCTION IN DNA/RNA UNWINDING, AND CATALYTIC ACTIVITY.
PubMed=21561811; DOI=10.1016/j.dnarep.2011.04.013;
Chakraborty P., Grosse F.;
"Human DHX9 helicase preferentially unwinds RNA-containing
displacement loops (R-loops) and G-quadruplexes.";
DNA Repair 10:654-665(2011).
[48]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH MAVS, AND DOUBLE
STRANDED RNA-BINDING (MICROBIAL INFECTION).
PubMed=21957149; DOI=10.4049/jimmunol.1101307;
Zhang Z., Yuan B., Lu N., Facchinetti V., Liu Y.J.;
"DHX9 pairs with IPS-1 to sense double-stranded RNA in myeloid
dendritic cells.";
J. Immunol. 187:4501-4508(2011).
[49]
FUNCTION IN MRNA TRANSLATION, AND INTERACTION WITH LIN28A.
PubMed=21247876; DOI=10.1093/nar/gkq1350;
Jin J., Jing W., Lei X.X., Feng C., Peng S., Boris-Lawrie K.,
Huang Y.;
"Evidence that Lin28 stimulates translation by recruiting RNA helicase
A to polysomes.";
Nucleic Acids Res. 39:3724-3734(2011).
[50]
FUNCTION IN MRNA TRANSLATION, INTERACTION WITH LARP6, MRNA-BINDING,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22190748; DOI=10.1261/rna.030288.111;
Manojlovic Z., Stefanovic B.;
"A novel role of RNA helicase A in regulation of translation of type I
collagen mRNAs.";
RNA 18:321-334(2012).
[51]
INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3.
PubMed=23640942; DOI=10.1515/hsz-2013-0111;
Wachter K., Kohn M., Stohr N., Huttelmaier S.;
"Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-
binding proteins) is modulated by distinct RNA-binding domains.";
Biol. Chem. 394:1077-1090(2013).
[52]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-321; SER-449
AND SER-506, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[53]
FUNCTION AS A TRIPLEX DNA HELICASE, CATALYTIC ACTIVITY, AND TRIPLEX
DNA-BINDING.
PubMed=24049074; DOI=10.1093/nar/gkt804;
Jain A., Bacolla A., Del Mundo I.M., Zhao J., Wang G., Vasquez K.M.;
"DHX9 helicase is involved in preventing genomic instability induced
by alternatively structured DNA in human cells.";
Nucleic Acids Res. 41:10345-10357(2013).
[54]
INTERACTION WITH LMX1B, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23308148; DOI=10.1371/journal.pone.0053122;
Hoekstra E.J., Mesman S., de Munnik W.A., Smidt M.P.;
"LMX1B is part of a transcriptional complex with PSPC1 and PSF.";
PLoS ONE 8:E53122-E53122(2013).
[55]
FUNCTION (MICROBIAL INFECTION).
PubMed=25149208; DOI=10.1016/j.bbagrm.2014.08.008;
Xing L., Niu M., Kleiman L.;
"Role of the OB-fold of RNA helicase A in the synthesis of HIV-1
RNA.";
Biochim. Biophys. Acta 1839:1069-1078(2014).
[56]
FUNCTION IN DNA/RNA UNWINDING, CATALYTIC ACTIVITY, AND DOMAINS.
PubMed=25062910; DOI=10.1016/j.bbapap.2014.07.001;
Xing L., Zhao X., Niu M., Kleiman L.;
"Helicase associated 2 domain is essential for helicase activity of
RNA helicase A.";
Biochim. Biophys. Acta 1844:1757-1764(2014).
[57]
FUNCTION IN DNA REPLICATION, CHROMATIN-BINDING, AND MUTAGENESIS OF
ASP-511; GLU-512 AND SER-543.
PubMed=24990949; DOI=10.1074/jbc.M114.568535;
Lee T., Di Paola D., Malina A., Mills J.R., Kreps A., Grosse F.,
Tang H., Zannis-Hadjopoulos M., Larsson O., Pelletier J.;
"Suppression of the DHX9 helicase induces premature senescence in
human diploid fibroblasts in a p53-dependent manner.";
J. Biol. Chem. 289:22798-22814(2014).
[58]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[59]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-146 AND ARG-1175, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[60]
FUNCTION (MICROBIAL INFECTION), AND RNA-BINDING (MICROBIAL INFECTION).
PubMed=27107641; DOI=10.1016/j.jmb.2016.04.011;
Boeras I., Song Z., Moran A., Franklin J., Brown W.C., Johnson M.,
Boris-Lawrie K., Heng X.;
"DHX9/RHA binding to the PBS-segment of the genomic RNA during HIV-1
assembly bolsters virion infectivity.";
J. Mol. Biol. 428:2418-2429(2016).
[61]
FUNCTION IN POST-TRANSCRIPTIONAL PROCESSING, INTERACTION WITH NUP98,
SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
MUTAGENESIS OF ILE-347 AND LYS-417.
PubMed=28221134; DOI=10.7554/eLife.18825;
Capitanio J.S., Montpetit B., Wozniak R.W.;
"Human Nup98 regulates the localization and activity of DExH/D-box
helicase DHX9.";
Elife 6:0-0(2017).
[62]
FUNCTION IN POST-TRANSCRIPTIONAL PROCESSING, INTERACTION WITH ADAR,
AND ALU RNA-BINDING.
PubMed=28355180; DOI=10.1038/nature21715;
Aktas T., Avsar Ilik I., Maticzka D., Bhardwaj V.,
Pessoa Rodrigues C., Mittler G., Manke T., Backofen R., Akhtar A.;
"DHX9 suppresses RNA processing defects originating from the Alu
invasion of the human genome.";
Nature 544:115-119(2017).
[63]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-697, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[64]
FUNCTION, AND INTERACTION WITH NLRP9.
PubMed=28636595; DOI=10.1038/nature22967;
Zhu S., Ding S., Wang P., Wei Z., Pan W., Palm N.W., Yang Y., Yu H.,
Li H.B., Wang G., Lei X., de Zoete M.R., Zhao J., Zheng Y., Chen H.,
Zhao Y., Jurado K.A., Feng N., Shan L., Kluger Y., Lu J., Abraham C.,
Fikrig E., Greenberg H.B., Flavell R.A.;
"Nlrp9b inflammasome restricts rotavirus infection in intestinal
epithelial cells.";
Nature 546:667-670(2017).
[65]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 329-563 IN COMPLEX WITH ADP
AND MANGANESE, NUCLEOTIDE-BINDING, AND CATALYTIC ACTIVITY.
PubMed=20510246; DOI=10.1016/j.jmb.2010.05.046;
Schutz P., Wahlberg E., Karlberg T., Hammarstrom M., Collins R.,
Flores A., Schuler H.;
"Crystal structure of human RNA helicase A (DHX9): structural basis
for unselective nucleotide base binding in a DEAD-box variant
protein.";
J. Mol. Biol. 400:768-782(2010).
[66]
X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-86 AND 169-263 IN COMPLEX
WITH SIRNA, DOUBLE-STRANDED RNA-BINDING, INTERACTION WITH AGO2 AND
TARBP2, AND MUTAGENESIS OF LYS-5; ASN-6; TYR-9; ASN-30; ASN-53;
LYS-54; LYS-55; LYS-182; ASN-186; GLN-187; HIS-207; ASN-234; LYS-235
AND LYS-236.
PubMed=23361462; DOI=10.1093/nar/gkt042;
Fu Q., Yuan Y.A.;
"Structural insights into RISC assembly facilitated by dsRNA-binding
domains of human RNA helicase A (DHX9).";
Nucleic Acids Res. 41:3457-3470(2013).
-!- FUNCTION: Multifunctional ATP-dependent nucleic acid helicase that
unwinds DNA and RNA in a 3' to 5' direction and that plays
important roles in many processes, such as DNA replication,
transcriptional activation, post-transcriptional RNA regulation,
mRNA translation and RNA-mediated gene silencing (PubMed:9111062,
PubMed:11416126, PubMed:12711669, PubMed:15355351,
PubMed:16680162, PubMed:17531811, PubMed:20669935,
PubMed:21561811, PubMed:24049074, PubMed:25062910,
PubMed:24990949, PubMed:28221134). Requires a 3'-single-stranded
tail as entry site for acid nuclei unwinding activities as well as
the binding and hydrolyzing of any of the four ribo- or deoxyribo-
nucleotide triphosphates (NTPs) (PubMed:1537828). Unwinds numerous
nucleic acid substrates such as double-stranded (ds) DNA and RNA,
DNA:RNA hybrids, DNA and RNA forks composed of either partially
complementary DNA duplexes or DNA:RNA hybrids, respectively, and
also DNA and RNA displacement loops (D- and R-loops), triplex-
helical DNA (H-DNA) structure and DNA and RNA-based G-quadruplexes
(PubMed:20669935, PubMed:21561811, PubMed:24049074). Binds dsDNA,
single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing
RNA (PubMed:9111062, PubMed:10198287). Binds also to circular
dsDNA or dsRNA of either linear and/or circular forms and
stimulates the relaxation of supercoiled DNAs catalyzed by
topoisomerase TOP2A (PubMed:12711669). Plays a role in DNA
replication at origins of replication and cell cycle progression
(PubMed:24990949). Plays a role as a transcriptional coactivator
acting as a bridging factor between polymerase II holoenzyme and
transcription factors or cofactors, such as BRCA1, CREBBP, RELA
and SMN1 (PubMed:11149922, PubMed:9323138, PubMed:9662397,
PubMed:11038348, PubMed:11416126, PubMed:15355351,
PubMed:28221134). Binds to the CDKN2A promoter (PubMed:11038348).
Plays several roles in post-transcriptional regulation of gene
expression (PubMed:28221134, PubMed:28355180). In cooperation with
NUP98, promotes pre-mRNA alternative splicing activities of a
subset of genes (PubMed:11402034, PubMed:16680162,
PubMed:28221134, PubMed:28355180). As component of a large PER
complex, is involved in the negative regulation of 3'
transcriptional termination of circadian target genes such as PER1
and NR1D1 and the control of the circadian rhythms (By
similarity). Acts also as a nuclear resolvase that is able to bind
and neutralize harmful massive secondary double-stranded RNA
structures formed by inverted-repeat Alu retrotransposon elements
that are inserted and transcribed as parts of genes during the
process of gene transposition (PubMed:28355180). Involved in the
positive regulation of nuclear export of constitutive transport
element (CTE)-containing unspliced mRNA (PubMed:9162007,
PubMed:10924507, PubMed:11402034). Component of the coding region
determinant (CRD)-mediated complex that promotes cytoplasmic MYC
mRNA stability (PubMed:19029303). Plays a role in mRNA translation
(PubMed:28355180). Positively regulates translation of selected
mRNAs through its binding to post-transcriptional control element
(PCE) in the 5'-untranslated region (UTR) (PubMed:16680162).
Involved with LARP6 in the translation stimulation of type I
collagen mRNAs for CO1A1 and CO1A2 through binding of a specific
stem-loop structure in their 5'-UTRs (PubMed:22190748). Stimulates
LIN28A-dependent mRNA translation probably by facilitating
ribonucleoprotein remodeling during the process of translation
(PubMed:21247876). Plays also a role as a small interfering
(siRNA)-loading factor involved in the RNA-induced silencing
complex (RISC) loading complex (RLC) assembly, and hence functions
in the RISC-mediated gene silencing process (PubMed:17531811).
Binds preferentially to short double-stranded RNA, such as those
produced during rotavirus intestinal infection (PubMed:28636595).
This interaction may mediate NLRP9 inflammasome activation and
trigger inflammatory response, including IL18 release and
pyroptosis (PubMed:28636595). Finally, mediates the attachment of
heterogeneous nuclear ribonucleoproteins (hnRNPs) to actin
filaments in the nucleus (PubMed:11687588).
{ECO:0000250|UniProtKB:O70133, ECO:0000269|PubMed:10198287,
ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:11038348,
ECO:0000269|PubMed:11149922, ECO:0000269|PubMed:11402034,
ECO:0000269|PubMed:11416126, ECO:0000269|PubMed:11687588,
ECO:0000269|PubMed:12711669, ECO:0000269|PubMed:15355351,
ECO:0000269|PubMed:1537828, ECO:0000269|PubMed:16680162,
ECO:0000269|PubMed:17531811, ECO:0000269|PubMed:19029303,
ECO:0000269|PubMed:20669935, ECO:0000269|PubMed:21247876,
ECO:0000269|PubMed:21561811, ECO:0000269|PubMed:22190748,
ECO:0000269|PubMed:24049074, ECO:0000269|PubMed:24990949,
ECO:0000269|PubMed:25062910, ECO:0000269|PubMed:28221134,
ECO:0000269|PubMed:28355180, ECO:0000269|PubMed:28636595,
ECO:0000269|PubMed:9111062, ECO:0000269|PubMed:9162007,
ECO:0000269|PubMed:9323138, ECO:0000269|PubMed:9662397}.
-!- FUNCTION: (Microbial infection) Plays a role in HIV-1 replication
and virion infectivity (PubMed:11096080, PubMed:19229320,
PubMed:25149208, PubMed:27107641). Enhances HIV-1 transcription by
facilitating the binding of RNA polymerase II holoenzyme to the
proviral DNA (PubMed:11096080, PubMed:25149208). Binds (via DRBM
domain 2) to the HIV-1 TAR RNA and stimulates HIV-1 transcription
of transactivation response element (TAR)-containing mRNAs
(PubMed:9892698, PubMed:11096080). Involved also in HIV-1 mRNA
splicing and transport (PubMed:25149208). Positively regulates
HIV-1 gag mRNA translation, through its binding to post-
transcriptional control element (PCE) in the 5'-untranslated
region (UTR) (PubMed:16680162). Binds (via DRBM domains) to a HIV-
1 double-stranded RNA region of the primer binding site (PBS)-
segment of the 5'-UTR, and hence stimulates DHX9 incorporation
into virions and virion infectivity (PubMed:27107641). Plays also
a role as a cytosolic viral MyD88-dependent DNA and RNA sensors in
plasmacytoid dendritic cells (pDCs), and hence induce antiviral
innate immune responses (PubMed:20696886, PubMed:21957149). Binds
(via the OB-fold region) to viral single-stranded DNA unmethylated
C-phosphate-G (CpG) oligonucleotide (PubMed:20696886).
{ECO:0000269|PubMed:11096080, ECO:0000269|PubMed:16680162,
ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:20696886,
ECO:0000269|PubMed:21957149, ECO:0000269|PubMed:25149208,
ECO:0000269|PubMed:27107641, ECO:0000269|PubMed:9892698}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{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}.
-!- SUBUNIT: Component of the coding region determinant (CRD)-mediated
complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1
(PubMed:19029303). Identified in a mRNP complex, at least composed
of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2,
PTBP2, STAU1, STAU2, SYNCRIP and YBX1 (PubMed:19029303).
Identified in a IGF2BP1-dependent mRNP granule complex containing
untranslated mRNAs (PubMed:17289661). The large PER complex
involved in the repression of transcriptional termination is
composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A
(active) (By similarity). Associates (via DRBM domains) with the
RISC complex; this association occurs in a small interfering
(siRNA)-dependent manner (PubMed:17531811, PubMed:23361462).
Associates with the SMN complex; this association induces
recruitment of DHX9 to the RNA polymerase II (ref.8). Associates
with polysomes in a LIN28A-dependent manner (PubMed:16680162,
PubMed:21247876). Interacts (via C-terminus) with ACTB; this
interaction is direct and mediates the attachment to nuclear
ribonucleoprotein complexes (PubMed:11687588). Interacts with ADAR
isoform 1; this interaction occurs in a RNA-independent manner
(PubMed:28355180). Interacts (via DRBM domains) with AGO2 (via
middle region); this interaction promotes active RISC assembly by
promoting the association of siRNA with AGO2 (PubMed:17531811,
PubMed:23361462). Interacts (via RGG region) with AKAP8L (via N-
terminus) (PubMed:11402034). Interacts with BRCA1 (via C-
terminus); this interaction is direct and links BRCA1 to the RNA
polymerase II holoenzyme (PubMed:9662397). Interacts (via N-
terminus) with CREBBP; this interaction mediates association with
RNA polymerase II holoenzyme and stimulates CREB-dependent
transcriptional activation (PubMed:9323138). Interacts (via N-
terminus) with EIF2AK2/PKR; this interaction is dependent upon the
activation of the kinase (PubMed:19229320). Interacts (via DRBM
domains) with DICER1 (PubMed:17531811). Interacts with H2AFX; this
interaction is direct, requires phosphorylation of histone H2AFX
on 'Ser-140' by PRKDC and promotes binding of DHX9 to
transcriptionally stalled sites on chromosomal DNA in response to
genotoxic stress (PubMed:15613478, PubMed:17498979). Interacts
with HNRNPC; this interaction is direct, enhanced probably by
their concomitant binding to RNA and mediates the attachment to
actin filaments (PubMed:11687588). Interacts (via RGG region) with
PRMT1 (PubMed:15084609). Interacts with IGF2BP1 (PubMed:17289661,
PubMed:23640942). Interacts with IGF2BP2, IGF2BP3
(PubMed:23640942). Interacts (via DRBM domains) with ILF3; this
interaction occurs in a RNA-independent manner (PubMed:12946349).
Interacts with Importin alpha/Importin beta receptor
(PubMed:16375861). Interacts with LARP6 (via C-terminus); this
interaction occurs in a mRNA-independent manner (PubMed:22190748).
Interacts (via N- and C-terminus) with LIN28A (via C-terminus);
this interaction occurs in a RNA-independent manner
(PubMed:21247876). Interacts with LMX1B (PubMed:23308148).
Interacts (via helicase C-terminal domain, HA2 and OB-fold
regions) with MAVS (via CARD domain); this interaction occurs in
both resting and double-stranded RNA poly(I:C)-induced cells
(PubMed:21957149). Interacts with MBD2; this interaction
stimulates transcriptional activation in a CREB-dependent manner
(PubMed:12665568). Interacts (via H2A and OB-fold regions) with
MYD88 (via TIR domain); this interaction is direct
(PubMed:20696886). Interacts with NLRP9 upon rotavirus infection;
this interaction may trigger NLRP9 inflammasome activation and
inflammatory response (PubMed:28636595). Interacts (via DRBM, OB-
fold and RGG regions) with NUP98 (via N-terminus); this
interaction occurs in a RNA-dependent manner and stimulates DHX9-
mediated ATPase activity and regulates transcription and splicing
of a subset of genes (PubMed:28221134). Interacts (via N-terminus)
with NXF1 (via N-terminus); this interaction is direct and
negatively regulates NXF1-mediated nuclear export of constitutive
transport element (CTE)-containing cellular mRNAs
(PubMed:10924507). Interacts with RELA; this interaction is direct
and activates NF-kappa-B-mediated transcription (PubMed:15355351).
Interacts (via MTAD region) with RNA polymerase II holoenzyme;
this interaction stimulates transcription activation in a CREB-
dependent manner (PubMed:11149922, PubMed:9323138,
PubMed:11416126). Interacts (via RGG region) with SMN1; this
interaction links SMN1 to the RNA polymerase II holoenzyme
(PubMed:11149922). Interacts with SP7 (PubMed:17303075). Interacts
(via DRBM domains) with TARBP2 (via DRBM first and second
domains); this interaction occurs in a small interfering (siRNA)-
dependent manner (PubMed:17531811, PubMed:23361462). Interacts
with TOP2A; this interaction occurs in a E2 enzyme UBE2I- and RNA-
dependent manner, negatively regulates DHX9-mediated double-
stranded DNA and RNA duplex helicase activity and stimulates
TOP2A-mediated supercoiled DNA relaxation activity
(PubMed:12711669). Interacts (via DRBM domains and C-terminus)
with WRN (via 3'-5' exonuclease domain); this interaction inhibits
the DNA-dependent NTPase and DNA helicase activities of DHX9 and
stimulates the 3'-5' exonuclease activity of WRN
(PubMed:15995249). Interacts with XRCC5; this interaction occurs
in a RNA-dependent manner (PubMed:14704337). Interacts with ZIC2
(via C2H2-type domain 3) (PubMed:17251188).
{ECO:0000250|UniProtKB:O70133, ECO:0000269|PubMed:10924507,
ECO:0000269|PubMed:11149922, ECO:0000269|PubMed:11402034,
ECO:0000269|PubMed:11416126, ECO:0000269|PubMed:11687588,
ECO:0000269|PubMed:12665568, ECO:0000269|PubMed:12711669,
ECO:0000269|PubMed:12946349, ECO:0000269|PubMed:14704337,
ECO:0000269|PubMed:15084609, ECO:0000269|PubMed:15355351,
ECO:0000269|PubMed:15613478, ECO:0000269|PubMed:15995249,
ECO:0000269|PubMed:16375861, ECO:0000269|PubMed:16680162,
ECO:0000269|PubMed:17251188, ECO:0000269|PubMed:17289661,
ECO:0000269|PubMed:17303075, ECO:0000269|PubMed:17498979,
ECO:0000269|PubMed:17531811, ECO:0000269|PubMed:19029303,
ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:20696886,
ECO:0000269|PubMed:21247876, ECO:0000269|PubMed:21957149,
ECO:0000269|PubMed:22190748, ECO:0000269|PubMed:23308148,
ECO:0000269|PubMed:23361462, ECO:0000269|PubMed:23640942,
ECO:0000269|PubMed:28221134, ECO:0000269|PubMed:28355180,
ECO:0000269|PubMed:28636595, ECO:0000269|PubMed:9323138,
ECO:0000269|PubMed:9662397}.
-!- INTERACTION:
P19525:EIF2AK2; NbExp=2; IntAct=EBI-352022, EBI-640775;
Q9UBU9:NXF1; NbExp=8; IntAct=EBI-352022, EBI-398874;
Q99873:PRMT1; NbExp=2; IntAct=EBI-352022, EBI-78738;
Q04206:RELA; NbExp=4; IntAct=EBI-352022, EBI-73886;
O14980:XPO1; NbExp=3; IntAct=EBI-352022, EBI-355867;
P67809:YBX1; NbExp=10; IntAct=EBI-352022, EBI-354065;
Q9HA38:ZMAT3; NbExp=3; IntAct=EBI-352022, EBI-2548480;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10198287,
ECO:0000269|PubMed:10207077, ECO:0000269|PubMed:11687588,
ECO:0000269|PubMed:16375861, ECO:0000269|PubMed:17303075,
ECO:0000269|PubMed:9162007}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:28221134}. Nucleus, nucleolus
{ECO:0000269|PubMed:12429849}. Cytoplasm
{ECO:0000269|PubMed:10198287, ECO:0000269|PubMed:10207077,
ECO:0000269|PubMed:16375861, ECO:0000269|PubMed:17289661,
ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:20696886,
ECO:0000269|PubMed:8690889, ECO:0000269|PubMed:9162007}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:17498979}. Note=Nucleoplasmic shuttling
protein (PubMed:10198287, PubMed:16375861, PubMed:10207077,
PubMed:9162007). Its nuclear import involves the nucleocytoplasmic
transport receptor Importin alpha/Importin beta receptor pathway
in a Ran-dependent manner (PubMed:16375861). In interphase,
localizes in nuclear stress granules and at perichromatin fibrils
and in cytoplasmic ribonucleoprotein granules (PubMed:10198287).
Colocalizes with WRN and H2AFX at centrosomes in a microtubule-
dependent manner following DNA damaging agent treatment
(PubMed:17498979). Excluded from the mitotic nucleus as early as
prophase and re-entered the nucleus at telophase
(PubMed:10198287). Recruited in diffuse and discrete intranuclear
foci (GLFG-body) in a NUP98-dependent manner (PubMed:28221134).
Colocalizes with SP7 in the nucleus (PubMed:17303075). Colocalizes
with ACTB at nuclear actin filaments inside the nucleus or at the
nuclear pore (PubMed:11687588). Colocalizes with HNRNPC at nuclear
ribonucleoprotein complex proteins in the nucleus
(PubMed:11687588). Localized in cytoplasmic mRNP granules
containing untranslated mRNAs (PubMed:17289661).
{ECO:0000269|PubMed:10198287, ECO:0000269|PubMed:10207077,
ECO:0000269|PubMed:11687588, ECO:0000269|PubMed:16375861,
ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17303075,
ECO:0000269|PubMed:17498979, ECO:0000269|PubMed:28221134,
ECO:0000269|PubMed:9162007}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q08211-1; Sequence=Displayed;
Name=2; Synonyms=Leukophysin, LKP;
IsoId=Q08211-2; Sequence=VSP_042314;
-!- DOMAIN: DRBM domains cooperate for the binding to nucleic acid but
not for unwinding helicase activity (PubMed:9111062,
PubMed:25062910). The helicase-associated domain-2 (HA2) region is
essential for the duplex RNA unwinding helicase activity
(PubMed:25062910). The minimal transactivation region (MTAD)
mediates interaction with the RNA polymerase II holoenzyme and
stimulates transcriptional activation in a CREB-dependent manner
(PubMed:11416126). The oligonucleotide- or oligosaccharide-binding
(OB-fold) and the repeated arginine and glycine-glycine (RGG)
regions are dispensable for both RNA-binding and unwinding
helicase activities (PubMed:25062910). The RGG region contains
both nuclear localization signal (NLS) and nuclear export signal
(NES) and is necessary and sufficient for nucleocytoplasmic
shuttling in a RNA-independent manner (PubMed:10207077,
PubMed:11149922). {ECO:0000269|PubMed:10207077,
ECO:0000269|PubMed:11149922, ECO:0000269|PubMed:11416126,
ECO:0000269|PubMed:25062910, ECO:0000269|PubMed:9111062}.
-!- PTM: Methylated (PubMed:15084609). PRMT1-mediated methylation of
undefined Arg residues in the RGG region is required for nuclear
import of DHX9 (PubMed:15084609). {ECO:0000269|PubMed:15084609}.
-!- PTM: Phosphorylated by PRKDC; phosphorylation occurs in a RNA-
dependent manner (PubMed:14704337). Phosphorylated by EIF2AK2/PKR;
this phosphorylation reduces its association with double-stranded
RNA (PubMed:19229320). {ECO:0000269|PubMed:14704337,
ECO:0000269|PubMed:19229320}.
-!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DHX9ID44879ch1q25.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L13848; AAB48855.1; -; mRNA.
EMBL; U03643; AAA03571.1; -; mRNA.
EMBL; Y10658; CAA71668.1; -; mRNA.
EMBL; AB451248; BAG70062.1; -; mRNA.
EMBL; AB451372; BAG70186.1; -; mRNA.
EMBL; AL355999; CAH71701.1; -; Genomic_DNA.
EMBL; AL662837; CAH71701.1; JOINED; Genomic_DNA.
EMBL; AL662837; CAI19277.1; -; Genomic_DNA.
EMBL; AL355999; CAI19277.1; JOINED; Genomic_DNA.
EMBL; CH471067; EAW91138.1; -; Genomic_DNA.
EMBL; BC025245; AAH25245.1; -; mRNA.
EMBL; BC058896; AAH58896.1; -; mRNA.
EMBL; BC107881; AAI07882.1; -; mRNA.
EMBL; BC137136; AAI37137.1; -; mRNA.
CCDS; CCDS41444.1; -. [Q08211-1]
RefSeq; NP_001348.2; NM_001357.4. [Q08211-1]
UniGene; Hs.191518; -.
PDB; 3LLM; X-ray; 2.80 A; A/B=329-563.
PDB; 3VYX; X-ray; 2.29 A; A=169-263.
PDB; 3VYY; X-ray; 2.90 A; A/B=1-86.
PDBsum; 3LLM; -.
PDBsum; 3VYX; -.
PDBsum; 3VYY; -.
ProteinModelPortal; Q08211; -.
SMR; Q08211; -.
BioGrid; 108025; 240.
CORUM; Q08211; -.
DIP; DIP-31504N; -.
IntAct; Q08211; 82.
MINT; MINT-5000572; -.
STRING; 9606.ENSP00000356520; -.
iPTMnet; Q08211; -.
PhosphoSitePlus; Q08211; -.
SwissPalm; Q08211; -.
BioMuta; DHX9; -.
DMDM; 116241330; -.
SWISS-2DPAGE; Q08211; -.
EPD; Q08211; -.
MaxQB; Q08211; -.
PaxDb; Q08211; -.
PeptideAtlas; Q08211; -.
PRIDE; Q08211; -.
TopDownProteomics; Q08211-1; -. [Q08211-1]
Ensembl; ENST00000367549; ENSP00000356520; ENSG00000135829. [Q08211-1]
GeneID; 1660; -.
KEGG; hsa:1660; -.
UCSC; uc001gpr.4; human. [Q08211-1]
CTD; 1660; -.
DisGeNET; 1660; -.
EuPathDB; HostDB:ENSG00000135829.16; -.
GeneCards; DHX9; -.
H-InvDB; HIX0001404; -.
H-InvDB; HIX0149309; -.
HGNC; HGNC:2750; DHX9.
HPA; CAB011819; -.
HPA; HPA028050; -.
HPA; HPA055684; -.
MIM; 603115; gene.
neXtProt; NX_Q08211; -.
OpenTargets; ENSG00000135829; -.
PharmGKB; PA27232; -.
eggNOG; KOG0920; Eukaryota.
eggNOG; COG1643; LUCA.
GeneTree; ENSGT00760000119189; -.
HOGENOM; HOG000247063; -.
HOVERGEN; HBG039429; -.
InParanoid; Q08211; -.
KO; K13184; -.
OMA; CSDHVAM; -.
OrthoDB; EOG091G0PKT; -.
PhylomeDB; Q08211; -.
TreeFam; TF313601; -.
BRENDA; 3.6.4.13; 2681.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
ChiTaRS; DHX9; human.
GeneWiki; RNA_Helicase_A; -.
GenomeRNAi; 1660; -.
PMAP-CutDB; Q08211; -.
PRO; PR:Q08211; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000135829; -.
CleanEx; HS_DHX9; -.
Genevisible; Q08211; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0035068; C:micro-ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
GO; GO:0097165; C:nuclear stress granule; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005726; C:perichromatin fibrils; IDA:UniProtKB.
GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
GO; GO:0005844; C:polysome; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0070578; C:RISC-loading complex; IMP:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IDA:UniProtKB.
GO; GO:0033681; F:ATP-dependent 3'-5' DNA/RNA helicase activity; IDA:UniProtKB.
GO; GO:0034459; F:ATP-dependent 3'-5' RNA helicase activity; IDA:UniProtKB.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; IMP:UniProtKB.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; IDA:UniProtKB.
GO; GO:0016887; F:ATPase activity; IMP:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003688; F:DNA replication origin binding; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
GO; GO:0061676; F:importin-alpha family protein binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0017111; F:nucleoside-triphosphatase activity; ISS:UniProtKB.
GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IDA:UniProtKB.
GO; GO:1905538; F:polysome binding; IDA:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; IMP:UniProtKB.
GO; GO:0001069; F:regulatory region RNA binding; IDA:UniProtKB.
GO; GO:1905172; F:RISC complex binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003724; F:RNA helicase activity; TAS:ProtInc.
GO; GO:0070063; F:RNA polymerase binding; IDA:UniProtKB.
GO; GO:0000993; F:RNA polymerase II core binding; IDA:UniProtKB.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; IMP:UniProtKB.
GO; GO:0001104; F:RNA polymerase II transcription cofactor activity; IMP:UniProtKB.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
GO; GO:0035613; F:RNA stem-loop binding; IDA:UniProtKB.
GO; GO:1990825; F:sequence-specific mRNA binding; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:1990518; F:single-stranded DNA-dependent ATP-dependent 3'-5' DNA helicase activity; IDA:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0035197; F:siRNA binding; IDA:UniProtKB.
GO; GO:0045142; F:triplex DNA binding; IDA:UniProtKB.
GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
GO; GO:0071360; P:cellular response to exogenous dsRNA; IMP:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:UniProtKB.
GO; GO:0070934; P:CRD-mediated mRNA stabilization; IMP:UniProtKB.
GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
GO; GO:0039695; P:DNA-templated viral transcription; IDA:UniProtKB.
GO; GO:0044806; P:G-quadruplex DNA unwinding; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
GO; GO:2000767; P:positive regulation of cytoplasmic translation; IMP:UniProtKB.
GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
GO; GO:0045740; P:positive regulation of DNA replication; IMP:UniProtKB.
GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; IMP:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:UniProtKB.
GO; GO:2000637; P:positive regulation of gene silencing by miRNA; IMP:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0045089; P:positive regulation of innate immune response; ISS:UniProtKB.
GO; GO:1902741; P:positive regulation of interferon-alpha secretion; IMP:UniProtKB.
GO; GO:0035549; P:positive regulation of interferon-beta secretion; IMP:UniProtKB.
GO; GO:0032741; P:positive regulation of interleukin-18 production; ISS:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IMP:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:1905698; P:positive regulation of polysome binding; IMP:UniProtKB.
GO; GO:0060760; P:positive regulation of response to cytokine stimulus; IMP:UniProtKB.
GO; GO:0046833; P:positive regulation of RNA export from nucleus; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; IMP:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
GO; GO:0050434; P:positive regulation of viral transcription; IDA:UniProtKB.
GO; GO:1904973; P:positive regulation of viral translation; IMP:UniProtKB.
GO; GO:1903608; P:protein localization to cytoplasmic stress granule; IMP:AgBase.
GO; GO:0070269; P:pyroptosis; ISS:UniProtKB.
GO; GO:2000765; P:regulation of cytoplasmic translation; IDA:UniProtKB.
GO; GO:0050691; P:regulation of defense response to virus by host; ISS:UniProtKB.
GO; GO:0050684; P:regulation of mRNA processing; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0006396; P:RNA processing; IBA:GO_Central.
GO; GO:0010501; P:RNA secondary structure unwinding; IDA:UniProtKB.
GO; GO:0070922; P:small RNA loading onto RISC; IMP:UniProtKB.
GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; IMP:UniProtKB.
CDD; cd00079; HELICc; 1.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR011709; DUF1605.
InterPro; IPR007502; Helicase-assoc_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00270; DEAD; 1.
Pfam; PF00035; dsrm; 2.
Pfam; PF04408; HA2; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF07717; OB_NTP_bind; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00358; DSRM; 2.
SMART; SM00847; HA2; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
PROSITE; PS50137; DS_RBD; 2.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
ATP-binding; Biological rhythms; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; DNA replication; DNA-binding;
Helicase; Hydrolase; Immunity; Inflammatory response; Innate immunity;
Isopeptide bond; Manganese; Metal-binding; Methylation;
mRNA processing; mRNA splicing; mRNA transport; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
RNA-binding; RNA-mediated gene silencing; Transcription;
Transcription regulation; Transcription termination;
Translation regulation; Transport; Ubl conjugation.
CHAIN 1 1270 ATP-dependent RNA helicase A.
/FTId=PRO_0000055157.
DOMAIN 3 71 DRBM 1. {ECO:0000255|PROSITE-
ProRule:PRU00266,
ECO:0000269|PubMed:23361462,
ECO:0000269|PubMed:9111062}.
DOMAIN 180 252 DRBM 2. {ECO:0000255|PROSITE-
ProRule:PRU00266,
ECO:0000269|PubMed:23361462,
ECO:0000269|PubMed:9111062}.
DOMAIN 398 564 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541,
ECO:0000269|PubMed:20510246}.
DOMAIN 636 809 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 411 419 ATP. {ECO:0000244|PDB:3LLM,
ECO:0000269|PubMed:11416126,
ECO:0000269|PubMed:20510246}.
REGION 1 250 Interaction with CREBBP.
{ECO:0000269|PubMed:9323138}.
REGION 5 9 siRNA-binding. {ECO:0000244|PDB:3VYY,
ECO:0000269|PubMed:23361462}.
REGION 53 55 siRNA-binding. {ECO:0000244|PDB:3VYY,
ECO:0000269|PubMed:23361462}.
REGION 182 186 siRNA-binding. {ECO:0000244|PDB:3VYX,
ECO:0000269|PubMed:23361462}.
REGION 230 325 Interaction with BRCA1.
{ECO:0000269|PubMed:9662397}.
REGION 234 236 siRNA-binding.
{ECO:0000305|PubMed:23361462}.
REGION 255 664 Necessary for interaction with RNA
polymerase II holoenzyme.
{ECO:0000269|PubMed:9323138}.
REGION 313 952 Necessary for interaction with H2AFX.
{ECO:0000269|PubMed:15613478}.
REGION 331 380 MTAD. {ECO:0000269|PubMed:11416126}.
REGION 398 809 Core helicase.
{ECO:0000305|PubMed:25062910}.
REGION 831 919 HA2. {ECO:0000269|PubMed:25062910}.
REGION 958 1074 OB-fold. {ECO:0000269|PubMed:20696886,
ECO:0000269|PubMed:25062910,
ECO:0000269|PubMed:25149208}.
REGION 1150 1270 RGG. {ECO:0000269|PubMed:10207077,
ECO:0000269|PubMed:25062910,
ECO:0000269|PubMed:25149208,
ECO:0000269|PubMed:9111062}.
MOTIF 511 514 DEIH box.
MOTIF 586 595 Nuclear localization signal (NLS1).
{ECO:0000255}.
MOTIF 1155 1173 Nuclear localization signal (NLS2).
{ECO:0000269|PubMed:16375861}.
METAL 418 418 Manganese. {ECO:0000244|PDB:3LLM,
ECO:0000269|PubMed:20510246}.
METAL 512 512 Manganese. {ECO:0000244|PDB:3LLM,
ECO:0000269|PubMed:20510246}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 146 146 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O70133}.
MOD_RES 146 146 N6-methyllysine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 191 191 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 199 199 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:23186163}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 506 506 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1024 1024 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1166 1166 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:O70133}.
MOD_RES 1175 1175 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1219 1219 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:O70133}.
MOD_RES 1235 1235 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:O70133}.
MOD_RES 1242 1242 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:O70133}.
MOD_RES 1249 1249 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:O70133}.
MOD_RES 1265 1265 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:O70133}.
CROSSLNK 697 697 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 1035 Missing (in isoform 2).
{ECO:0000303|PubMed:19054851,
ECO:0000303|PubMed:8690889}.
/FTId=VSP_042314.
VARIANT 894 894 I -> V (in dbSNP:rs1049264).
{ECO:0000269|PubMed:8344961}.
/FTId=VAR_052179.
MUTAGEN 5 5 K->A: Reduces siRNA-binding and
interaction with AGO2; when associated
with A-6. {ECO:0000269|PubMed:23361462}.
MUTAGEN 6 6 N->A: Reduces siRNA-binding; when
associated with A-5.
{ECO:0000269|PubMed:23361462}.
MUTAGEN 9 9 Y->A: Inhibits siRNA-binding and
interaction with AGO2.
{ECO:0000269|PubMed:23361462}.
MUTAGEN 30 30 N->A: Does not reduce siRNA-binding and
interaction with AGO2.
{ECO:0000269|PubMed:23361462}.
MUTAGEN 53 53 N->A: Inhibits siRNA-binding and
decreases interaction with AGO2; when
associated with A-54 and A-55.
{ECO:0000269|PubMed:23361462}.
MUTAGEN 54 54 K->A: Inhibits siRNA-binding and
decreases interaction with AGO2; when
associated with A-53 and A-55.
{ECO:0000269|PubMed:23361462}.
MUTAGEN 55 55 K->A: Inhibits siRNA-binding and
decreases interaction with AGO2; when
associated with A-53 and A-54.
{ECO:0000269|PubMed:23361462}.
MUTAGEN 182 182 K->A: Reduces siRNA-binding and
interaction with AGO2.
{ECO:0000269|PubMed:23361462}.
MUTAGEN 186 186 N->A: Reduces siRNA-binding and
interaction with AGO2; when associated
with A-187.
{ECO:0000269|PubMed:23361462}.
MUTAGEN 187 187 Q->A: Reduces siRNA-binding and
interaction with AGO2; when associated
with A-186.
{ECO:0000269|PubMed:23361462}.
MUTAGEN 207 207 H->A: Reduces siRNA-binding and
interaction with AGO2.
{ECO:0000269|PubMed:23361462}.
MUTAGEN 234 234 N->A: Inhibits siRNA-binding and
interaction with AGO2; when associated
with A-235 and A-236.
{ECO:0000269|PubMed:23361462}.
MUTAGEN 235 235 K->A: Inhibits siRNA-binding and
interaction with AGO2; when associated
with A-234 and A-236.
{ECO:0000269|PubMed:23361462}.
MUTAGEN 236 236 K->A: Inhibits siRNA-binding and
interaction with AGO2; when associated
with A-234 and A-235.
{ECO:0000269|PubMed:23361462}.
MUTAGEN 332 332 W->A: Abrogates transcriptional
activation by the MTAD region. No change
in RNA polymerase II holoenzyme binding.
{ECO:0000269|PubMed:11416126}.
MUTAGEN 339 339 W->A: Abrogates transcriptional
activation and RNA polymerase II binding
by the MTAD region. No change in ATP
binding and ATPase activities.
{ECO:0000269|PubMed:11416126}.
MUTAGEN 342 342 W->A: Abrogates transcriptional
activation by the MTAD region. No change
in RNA polymerase II holoenzyme binding.
{ECO:0000269|PubMed:11416126}.
MUTAGEN 347 347 I->A: Reduces NUP98-induced mRNA
transcription and alternative splicing
activities.
{ECO:0000269|PubMed:28221134}.
MUTAGEN 417 417 K->R,N: Inhibits interaction with AGO2,
DICER1 and TARBP2. Abrogates helicase
activity and transcriptional activation.
Does not inhibit binding to origins of
DNA replication.
{ECO:0000269|PubMed:15355351,
ECO:0000269|PubMed:17531811,
ECO:0000269|PubMed:24990949,
ECO:0000269|PubMed:9323138}.
MUTAGEN 417 417 K->R: Reduces NUP98-induced mRNA
transcription and alternative splicing
activities.
{ECO:0000269|PubMed:28221134}.
MUTAGEN 511 511 D->A: Does not inhibit binding to origins
of DNA replication; when associated with
A-512. {ECO:0000269|PubMed:24990949}.
MUTAGEN 512 512 E->A: Does not inhibit binding to origins
of DNA replication; when associated with
A-511. {ECO:0000269|PubMed:24990949}.
MUTAGEN 543 543 S->L: Does not inhibit binding to origins
of DNA replication.
{ECO:0000269|PubMed:24990949}.
MUTAGEN 1160 1160 R->A: Localizes in the nucleus and
interacts with the importin complex.
{ECO:0000269|PubMed:16375861}.
MUTAGEN 1163 1163 K->A: Localizes in the cytoplasm and does
not interact with the importin complex.
{ECO:0000269|PubMed:16375861}.
MUTAGEN 1163 1163 Missing: Abolishes nuclear localization.
{ECO:0000269|PubMed:10207077}.
MUTAGEN 1166 1166 R->A: Localizes in the nucleus and the
cytoplasm and interacts weakly with the
importin complex.
{ECO:0000269|PubMed:16375861}.
MUTAGEN 1166 1166 R->L: Abolishes nuclear localization.
{ECO:0000269|PubMed:10207077}.
MUTAGEN 1166 1166 Missing: Abolishes nuclear localization.
{ECO:0000269|PubMed:10207077}.
CONFLICT 20 20 S -> T (in Ref. 1; AAB48855).
{ECO:0000305}.
CONFLICT 108 109 TM -> HH (in Ref. 1; AAB48855).
{ECO:0000305}.
CONFLICT 114 116 PPH -> LHI (in Ref. 1; AAB48855).
{ECO:0000305}.
CONFLICT 186 186 N -> I (in Ref. 1; AAB48855).
{ECO:0000305}.
CONFLICT 260 260 S -> T (in Ref. 1; AAB48855).
{ECO:0000305}.
CONFLICT 478 478 I -> V (in Ref. 1; AAB48855).
{ECO:0000305}.
CONFLICT 521 521 D -> S (in Ref. 1; AAB48855).
{ECO:0000305}.
CONFLICT 541 541 L -> F (in Ref. 1; AAB48855).
{ECO:0000305}.
CONFLICT 560 565 IIEVYG -> SLKLW (in Ref. 1; AAB48855).
{ECO:0000305}.
CONFLICT 590 590 D -> K (in Ref. 5; AAH25245).
{ECO:0000305}.
CONFLICT 749 749 A -> S (in Ref. 1; AAB48855 and 3;
CAA71668). {ECO:0000305}.
CONFLICT 768 770 VRP -> STA (in Ref. 1; AAB48855 and 3;
CAA71668). {ECO:0000305}.
CONFLICT 828 828 A -> G (in Ref. 5; AAI07882).
{ECO:0000305}.
CONFLICT 899 899 R -> Q (in Ref. 1; AAB48855).
{ECO:0000305}.
CONFLICT 1037 1037 K -> N (in Ref. 1; AAB48855).
{ECO:0000305}.
CONFLICT 1063 1063 T -> P (in Ref. 1; AAB48855 and 3;
CAA71668). {ECO:0000305}.
CONFLICT 1140 1140 R -> E (in Ref. 1; AAB48855).
{ECO:0000305}.
CONFLICT 1204 1211 NSFRAGYG -> TPSGRIC (in Ref. 1;
AAB48855). {ECO:0000305}.
CONFLICT 1261 1270 FGQGRGGGGY -> LDIEEEVAAIKLGYVSSVCRQ (in
Ref. 1; AAB48855). {ECO:0000305}.
HELIX 4 14 {ECO:0000244|PDB:3VYY}.
STRAND 20 28 {ECO:0000244|PDB:3VYY}.
STRAND 31 39 {ECO:0000244|PDB:3VYY}.
STRAND 47 53 {ECO:0000244|PDB:3VYY}.
HELIX 54 71 {ECO:0000244|PDB:3VYY}.
HELIX 77 79 {ECO:0000244|PDB:3VYY}.
HELIX 170 173 {ECO:0000244|PDB:3VYX}.
TURN 178 180 {ECO:0000244|PDB:3VYX}.
HELIX 181 191 {ECO:0000244|PDB:3VYX}.
STRAND 199 204 {ECO:0000244|PDB:3VYX}.
HELIX 206 208 {ECO:0000244|PDB:3VYX}.
STRAND 210 218 {ECO:0000244|PDB:3VYX}.
HELIX 220 222 {ECO:0000244|PDB:3VYX}.
STRAND 223 234 {ECO:0000244|PDB:3VYX}.
HELIX 235 252 {ECO:0000244|PDB:3VYX}.
TURN 341 344 {ECO:0000244|PDB:3LLM}.
TURN 351 354 {ECO:0000244|PDB:3LLM}.
HELIX 357 374 {ECO:0000244|PDB:3LLM}.
HELIX 376 386 {ECO:0000244|PDB:3LLM}.
HELIX 389 393 {ECO:0000244|PDB:3LLM}.
HELIX 394 403 {ECO:0000244|PDB:3LLM}.
STRAND 405 410 {ECO:0000244|PDB:3LLM}.
HELIX 417 431 {ECO:0000244|PDB:3LLM}.
HELIX 435 437 {ECO:0000244|PDB:3LLM}.
STRAND 439 446 {ECO:0000244|PDB:3LLM}.
HELIX 447 459 {ECO:0000244|PDB:3LLM}.
TURN 460 462 {ECO:0000244|PDB:3LLM}.
STRAND 467 473 {ECO:0000244|PDB:3LLM}.
STRAND 476 478 {ECO:0000244|PDB:3LLM}.
STRAND 482 490 {ECO:0000244|PDB:3LLM}.
HELIX 491 500 {ECO:0000244|PDB:3LLM}.
STRAND 507 510 {ECO:0000244|PDB:3LLM}.
HELIX 518 533 {ECO:0000244|PDB:3LLM}.
STRAND 537 543 {ECO:0000244|PDB:3LLM}.
HELIX 549 554 {ECO:0000244|PDB:3LLM}.
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


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