Full text data of DHX9
DHX9
(DDX9, LKP, NDH2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
ATP-dependent RNA helicase A; RHA; 3.6.4.13 (DEAH box protein 9; Leukophysin; LKP; Nuclear DNA helicase II; NDH II)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
ATP-dependent RNA helicase A; RHA; 3.6.4.13 (DEAH box protein 9; Leukophysin; LKP; Nuclear DNA helicase II; NDH II)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q08211
ID DHX9_HUMAN Reviewed; 1270 AA.
AC Q08211; B2RNV4; Q05CI5; Q12803; Q32Q22; Q5VY62; Q6PD69; Q99556;
read moreDT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 4.
DT 22-JAN-2014, entry version 153.
DE RecName: Full=ATP-dependent RNA helicase A;
DE Short=RHA;
DE EC=3.6.4.13;
DE AltName: Full=DEAH box protein 9;
DE AltName: Full=Leukophysin;
DE Short=LKP;
DE AltName: Full=Nuclear DNA helicase II;
DE Short=NDH II;
GN Name=DHX9; Synonyms=DDX9, LKP, NDH2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP VARIANT VAL-894.
RX PubMed=8344961;
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
RT cytotoxic T cell granules and vesicles.";
RL J. Immunol. 156:2026-2035(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PARTIAL PROTEIN SEQUENCE, INTERACTION WITH SMN1, AND IDENTIFICATION BY
RP 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
RT and RNA polymerase II.";
RL J. Cell Biol. 152:75-85(2001).
RN [9]
RP INTERACTION WITH CREBBP AND RNA POLYMERASE II, AND MUTAGENESIS OF
RP 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.,
RA Parvin J.D., Montminy M.;
RT "RNA helicase A mediates association of CBP with RNA polymerase II.";
RL Cell 90:1107-1112(1997).
RN [10]
RP 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
RT via RNA helicase A.";
RL Nat. Genet. 19:254-256(1998).
RN [11]
RP DOMAIN NTD, AND MUTAGENESIS OF LYS-1163 AND ARG-1166.
RX PubMed=10207077;
RA Tang H., McDonald D., Middlesworth T., Hope T.J., Wong-Staal F.;
RT "The carboxyl terminus of RNA helicase A contains a bidirectional
RT nuclear transport domain.";
RL Mol. Cell. Biol. 19:3540-3550(1999).
RN [12]
RP DOMAIN MTAD, AND 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
RP 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 [14]
RP 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 [15]
RP INTERACTION WITH TOP2A.
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 [16]
RP INTERACTION WITH RELA, AND 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.,
RA Wong-Staal F., Okamoto T.;
RT "RNA helicase A interacts with nuclear factor kappaB p65 and functions
RT as a transcriptional coactivator.";
RL Eur. J. Biochem. 271:3741-3751(2004).
RN [17]
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
RT helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent
RT manner.";
RL Nucleic Acids Res. 32:1-10(2004).
RN [18]
RP METHYLATION.
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 [19]
RP INTERACTION WITH H2AFX.
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
RT of gamma-H2AX with Ku70 and nuclear DNA helicase II.";
RL J. Biol. Chem. 280:9586-9594(2005).
RN [20]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1,
RP AND 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND MASS
RP SPECTROMETRY.
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 [23]
RP FUNCTION, INTERACTION WITH EIF2AK2, AND PHOSPHORYLATION.
RX PubMed=19229320; DOI=10.1371/journal.ppat.1000311;
RA Sadler A.J., Latchoumanin O., Hawkes D., Mak J., Williams B.R.;
RT "An antiviral response directed by PKR phosphorylation of the RNA
RT helicase A.";
RL PLoS Pathog. 5:E1000311-E1000311(2009).
RN [24]
RP FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX,
RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M.,
RA Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic
RT RNPs.";
RL RNA 15:104-115(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191; LYS-199 AND LYS-1024,
RP AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [27]
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.,
RA Buerckstuemmer T., 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 [28]
RP FUNCTION IN COLLAGEN MRNA STABILIZATION, AND INTERACTION WITH LARP6.
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 [29]
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-
RT binding proteins) is modulated by distinct RNA-binding domains.";
RL Biol. Chem. 394:1077-1090(2013).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 329-563 IN COMPLEX WITH ADP,
RP 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.,
RA Flores A., Schuler H.;
RT "Crystal structure of human RNA helicase A (DHX9): structural basis
RT for unselective nucleotide base binding in a DEAD-box variant
RT protein.";
RL J. Mol. Biol. 400:768-782(2010).
CC -!- FUNCTION: Unwinds double-stranded DNA and RNA in a 3' to 5'
CC direction. Alteration of secondary structure may subsequently
CC influence interactions with proteins or other nucleic acids.
CC Functions as a transcriptional activator. Component of the CRD-
CC mediated complex that promotes MYC mRNA stability. Involved with
CC LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and
CC CO1A2. Positively regulates HIV-1 LTR-directed gene expression.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Interacts with ZIC2, IGF2BP1, IGF2BP2, IGF2BP3, MBD2,
CC HRMT1L2/PRMT1, RELA and LARP6. Can also interact with XRCC5 and
CC with TOP2A in an RNA dependent manner; these interactions may be
CC indirect. Interaction with TOP2A is promoted by UBC9. Interacts
CC with histone H2AFX and this requires phosphorylation of H2AFX on
CC 'Ser-139'. Interacts (via N-terminus) with EIF2AK2/PKR and this
CC interaction is dependent upon the activation of the kinase.
CC Component of the coding region determinant (CRD)-mediated complex,
CC composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. May act to
CC directly link BRCA1, CREBBP or SMN1 and the RNA polymerase II
CC complex. Identified in a mRNP complex, at least composed of DHX9,
CC DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1,
CC STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP
CC granule complex containing untranslated mRNAs.
CC -!- INTERACTION:
CC P19525:EIF2AK2; NbExp=2; IntAct=EBI-352022, EBI-640775;
CC Q9UBU9:NXF1; NbExp=8; IntAct=EBI-352022, EBI-398874;
CC Q99873:PRMT1; NbExp=2; IntAct=EBI-352022, EBI-78738;
CC Q04206:RELA; NbExp=4; IntAct=EBI-352022, EBI-73886;
CC P67809:YBX1; NbExp=5; IntAct=EBI-352022, EBI-354065;
CC Q9HA38:ZMAT3; NbExp=3; IntAct=EBI-352022, EBI-2548480;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm.
CC Note=Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs. Can shuttle between nucleus and cytoplasm.
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: The MTAD domain mediates interaction with the RNA
CC polymerase II holoenzyme. The NTD domain is necessary and
CC sufficient for nucleo-cytoplasmic shuttling and interaction with
CC HRMT1L2 and SMN1.
CC -!- PTM: Methylated. HRMT1L2 mediated methylation of undefined Arg
CC residues in the NTD is required for nuclear localization.
CC -!- PTM: May be phosphorylated by PRKDC/XRCC7. Phosphorylated by
CC EIF2AK2/PKR and this phosphorylation perturbs its association with
CC dsRNA.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC subfamily.
CC -!- SIMILARITY: Contains 2 DRBM (double-stranded RNA-binding) domains.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DHX9ID702ch1q25.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; CAH71701.1; -; Genomic_DNA.
DR EMBL; AL662837; CAH71701.1; JOINED; Genomic_DNA.
DR EMBL; AL662837; CAI19277.1; -; Genomic_DNA.
DR EMBL; AL355999; CAI19277.1; JOINED; 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 RefSeq; NP_001348.2; NM_001357.4.
DR UniGene; Hs.191518; -.
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 ProteinModelPortal; Q08211; -.
DR SMR; Q08211; 1-86, 169-263, 329-1071.
DR DIP; DIP-31504N; -.
DR IntAct; Q08211; 47.
DR MINT; MINT-5000572; -.
DR STRING; 9606.ENSP00000356520; -.
DR PhosphoSite; Q08211; -.
DR DMDM; 116241330; -.
DR SWISS-2DPAGE; Q08211; -.
DR PaxDb; Q08211; -.
DR PRIDE; Q08211; -.
DR Ensembl; ENST00000367549; ENSP00000356520; ENSG00000135829.
DR GeneID; 1660; -.
DR KEGG; hsa:1660; -.
DR UCSC; uc001gpr.3; human.
DR CTD; 1660; -.
DR GeneCards; GC01P182808; -.
DR H-InvDB; HIX0001404; -.
DR H-InvDB; HIX0149309; -.
DR HGNC; HGNC:2750; DHX9.
DR HPA; CAB011819; -.
DR HPA; HPA028050; -.
DR MIM; 603115; gene.
DR neXtProt; NX_Q08211; -.
DR PharmGKB; PA27232; -.
DR eggNOG; COG1643; -.
DR HOGENOM; HOG000247063; -.
DR HOVERGEN; HBG039429; -.
DR InParanoid; Q08211; -.
DR KO; K13184; -.
DR OMA; VDDWIRL; -.
DR OrthoDB; EOG76471V; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RNA_Helicase_A; -.
DR GenomeRNAi; 1660; -.
DR NextBio; 6832; -.
DR PMAP-CutDB; Q08211; -.
DR PRO; PR:Q08211; -.
DR Bgee; Q08211; -.
DR CleanEx; HS_DHX9; -.
DR Genevestigator; Q08211; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc.
DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; TAS:ProtInc.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
DR GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
DR Gene3D; 3.30.160.20; -; 2.
DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014720; dsRNA-bd_dom.
DR InterPro; IPR011709; DUF1605.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Helicase; Hydrolase; Methylation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1 1270 ATP-dependent RNA helicase A.
FT /FTId=PRO_0000055157.
FT DOMAIN 3 71 DRBM 1.
FT DOMAIN 180 252 DRBM 2.
FT DOMAIN 398 564 Helicase ATP-binding.
FT DOMAIN 636 809 Helicase C-terminal.
FT NP_BIND 411 419 ATP.
FT REGION 1 250 Interaction with CREBBP.
FT REGION 230 325 Interaction with BRCA1.
FT REGION 331 380 MTAD.
FT REGION 1151 1260 NTD.
FT MOTIF 511 514 DEIH box.
FT MOTIF 586 595 Nuclear localization signal (Potential).
FT MOD_RES 87 87 Phosphoserine.
FT MOD_RES 191 191 N6-acetyllysine.
FT MOD_RES 199 199 N6-acetyllysine.
FT MOD_RES 321 321 Phosphoserine.
FT MOD_RES 1024 1024 N6-acetyllysine.
FT VAR_SEQ 1 1035 Missing (in isoform 2).
FT /FTId=VSP_042314.
FT VARIANT 894 894 I -> V (in dbSNP:rs1049264).
FT /FTId=VAR_052179.
FT MUTAGEN 332 332 W->A: Abrogates transcriptional
FT activation by the MTAD domain.
FT MUTAGEN 339 339 W->A: Abrogates transcriptional
FT activation and RNA polymerase II binding
FT by the MTAD domain.
FT MUTAGEN 342 342 W->A: Abrogates transcriptional
FT activation by the MTAD domain.
FT MUTAGEN 417 417 K->R: Abrogates transcriptional
FT activation.
FT MUTAGEN 1163 1163 Missing: Abolishes nuclear localization.
FT MUTAGEN 1166 1166 R->L: Abolishes nuclear localization.
FT MUTAGEN 1166 1166 Missing: Abolishes nuclear localization.
FT CONFLICT 20 20 S -> T (in Ref. 1; AAB48855).
FT CONFLICT 108 109 TM -> HH (in Ref. 1; AAB48855).
FT CONFLICT 114 116 PPH -> LHI (in Ref. 1; AAB48855).
FT CONFLICT 186 186 N -> I (in Ref. 1; AAB48855).
FT CONFLICT 260 260 S -> T (in Ref. 1; AAB48855).
FT CONFLICT 478 478 I -> V (in Ref. 1; AAB48855).
FT CONFLICT 521 521 D -> S (in Ref. 1; AAB48855).
FT CONFLICT 541 541 L -> F (in Ref. 1; AAB48855).
FT CONFLICT 560 565 IIEVYG -> SLKLW (in Ref. 1; AAB48855).
FT CONFLICT 590 590 D -> K (in Ref. 5; AAH25245).
FT CONFLICT 749 749 A -> S (in Ref. 1; AAB48855 and 3;
FT CAA71668).
FT CONFLICT 768 770 VRP -> STA (in Ref. 1; AAB48855 and 3;
FT CAA71668).
FT CONFLICT 828 828 A -> G (in Ref. 5; AAI07882).
FT CONFLICT 899 899 R -> Q (in Ref. 1; AAB48855).
FT CONFLICT 1037 1037 K -> N (in Ref. 1; AAB48855).
FT CONFLICT 1063 1063 T -> P (in Ref. 1; AAB48855 and 3;
FT CAA71668).
FT CONFLICT 1140 1140 R -> E (in Ref. 1; AAB48855).
FT CONFLICT 1204 1211 NSFRAGYG -> TPSGRIC (in Ref. 1;
FT AAB48855).
FT CONFLICT 1261 1270 FGQGRGGGGY -> LDIEEEVAAIKLGYVSSVCRQ (in
FT Ref. 1; AAB48855).
FT HELIX 4 14
FT STRAND 20 28
FT STRAND 31 39
FT STRAND 47 53
FT HELIX 54 71
FT HELIX 77 79
FT HELIX 170 173
FT TURN 178 180
FT HELIX 181 191
FT STRAND 199 204
FT HELIX 206 208
FT STRAND 210 218
FT HELIX 220 222
FT STRAND 223 234
FT HELIX 235 252
FT TURN 341 344
FT TURN 351 354
FT HELIX 357 374
FT HELIX 376 386
FT HELIX 389 393
FT HELIX 394 403
FT STRAND 405 410
FT HELIX 417 431
FT HELIX 435 437
FT STRAND 439 446
FT HELIX 447 459
FT TURN 460 462
FT STRAND 467 473
FT STRAND 476 478
FT STRAND 482 490
FT HELIX 491 500
FT STRAND 507 510
FT HELIX 518 533
FT STRAND 537 543
FT HELIX 549 554
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
//
ID DHX9_HUMAN Reviewed; 1270 AA.
AC Q08211; B2RNV4; Q05CI5; Q12803; Q32Q22; Q5VY62; Q6PD69; Q99556;
read moreDT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 4.
DT 22-JAN-2014, entry version 153.
DE RecName: Full=ATP-dependent RNA helicase A;
DE Short=RHA;
DE EC=3.6.4.13;
DE AltName: Full=DEAH box protein 9;
DE AltName: Full=Leukophysin;
DE Short=LKP;
DE AltName: Full=Nuclear DNA helicase II;
DE Short=NDH II;
GN Name=DHX9; Synonyms=DDX9, LKP, NDH2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP VARIANT VAL-894.
RX PubMed=8344961;
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
RT cytotoxic T cell granules and vesicles.";
RL J. Immunol. 156:2026-2035(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PARTIAL PROTEIN SEQUENCE, INTERACTION WITH SMN1, AND IDENTIFICATION BY
RP 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
RT and RNA polymerase II.";
RL J. Cell Biol. 152:75-85(2001).
RN [9]
RP INTERACTION WITH CREBBP AND RNA POLYMERASE II, AND MUTAGENESIS OF
RP 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.,
RA Parvin J.D., Montminy M.;
RT "RNA helicase A mediates association of CBP with RNA polymerase II.";
RL Cell 90:1107-1112(1997).
RN [10]
RP 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
RT via RNA helicase A.";
RL Nat. Genet. 19:254-256(1998).
RN [11]
RP DOMAIN NTD, AND MUTAGENESIS OF LYS-1163 AND ARG-1166.
RX PubMed=10207077;
RA Tang H., McDonald D., Middlesworth T., Hope T.J., Wong-Staal F.;
RT "The carboxyl terminus of RNA helicase A contains a bidirectional
RT nuclear transport domain.";
RL Mol. Cell. Biol. 19:3540-3550(1999).
RN [12]
RP DOMAIN MTAD, AND 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
RP 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 [14]
RP 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 [15]
RP INTERACTION WITH TOP2A.
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 [16]
RP INTERACTION WITH RELA, AND 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.,
RA Wong-Staal F., Okamoto T.;
RT "RNA helicase A interacts with nuclear factor kappaB p65 and functions
RT as a transcriptional coactivator.";
RL Eur. J. Biochem. 271:3741-3751(2004).
RN [17]
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
RT helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent
RT manner.";
RL Nucleic Acids Res. 32:1-10(2004).
RN [18]
RP METHYLATION.
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 [19]
RP INTERACTION WITH H2AFX.
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
RT of gamma-H2AX with Ku70 and nuclear DNA helicase II.";
RL J. Biol. Chem. 280:9586-9594(2005).
RN [20]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1,
RP AND 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND MASS
RP SPECTROMETRY.
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 [23]
RP FUNCTION, INTERACTION WITH EIF2AK2, AND PHOSPHORYLATION.
RX PubMed=19229320; DOI=10.1371/journal.ppat.1000311;
RA Sadler A.J., Latchoumanin O., Hawkes D., Mak J., Williams B.R.;
RT "An antiviral response directed by PKR phosphorylation of the RNA
RT helicase A.";
RL PLoS Pathog. 5:E1000311-E1000311(2009).
RN [24]
RP FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX,
RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M.,
RA Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic
RT RNPs.";
RL RNA 15:104-115(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191; LYS-199 AND LYS-1024,
RP AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [27]
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.,
RA Buerckstuemmer T., 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 [28]
RP FUNCTION IN COLLAGEN MRNA STABILIZATION, AND INTERACTION WITH LARP6.
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 [29]
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-
RT binding proteins) is modulated by distinct RNA-binding domains.";
RL Biol. Chem. 394:1077-1090(2013).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 329-563 IN COMPLEX WITH ADP,
RP 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.,
RA Flores A., Schuler H.;
RT "Crystal structure of human RNA helicase A (DHX9): structural basis
RT for unselective nucleotide base binding in a DEAD-box variant
RT protein.";
RL J. Mol. Biol. 400:768-782(2010).
CC -!- FUNCTION: Unwinds double-stranded DNA and RNA in a 3' to 5'
CC direction. Alteration of secondary structure may subsequently
CC influence interactions with proteins or other nucleic acids.
CC Functions as a transcriptional activator. Component of the CRD-
CC mediated complex that promotes MYC mRNA stability. Involved with
CC LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and
CC CO1A2. Positively regulates HIV-1 LTR-directed gene expression.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Interacts with ZIC2, IGF2BP1, IGF2BP2, IGF2BP3, MBD2,
CC HRMT1L2/PRMT1, RELA and LARP6. Can also interact with XRCC5 and
CC with TOP2A in an RNA dependent manner; these interactions may be
CC indirect. Interaction with TOP2A is promoted by UBC9. Interacts
CC with histone H2AFX and this requires phosphorylation of H2AFX on
CC 'Ser-139'. Interacts (via N-terminus) with EIF2AK2/PKR and this
CC interaction is dependent upon the activation of the kinase.
CC Component of the coding region determinant (CRD)-mediated complex,
CC composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. May act to
CC directly link BRCA1, CREBBP or SMN1 and the RNA polymerase II
CC complex. Identified in a mRNP complex, at least composed of DHX9,
CC DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1,
CC STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP
CC granule complex containing untranslated mRNAs.
CC -!- INTERACTION:
CC P19525:EIF2AK2; NbExp=2; IntAct=EBI-352022, EBI-640775;
CC Q9UBU9:NXF1; NbExp=8; IntAct=EBI-352022, EBI-398874;
CC Q99873:PRMT1; NbExp=2; IntAct=EBI-352022, EBI-78738;
CC Q04206:RELA; NbExp=4; IntAct=EBI-352022, EBI-73886;
CC P67809:YBX1; NbExp=5; IntAct=EBI-352022, EBI-354065;
CC Q9HA38:ZMAT3; NbExp=3; IntAct=EBI-352022, EBI-2548480;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm.
CC Note=Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs. Can shuttle between nucleus and cytoplasm.
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: The MTAD domain mediates interaction with the RNA
CC polymerase II holoenzyme. The NTD domain is necessary and
CC sufficient for nucleo-cytoplasmic shuttling and interaction with
CC HRMT1L2 and SMN1.
CC -!- PTM: Methylated. HRMT1L2 mediated methylation of undefined Arg
CC residues in the NTD is required for nuclear localization.
CC -!- PTM: May be phosphorylated by PRKDC/XRCC7. Phosphorylated by
CC EIF2AK2/PKR and this phosphorylation perturbs its association with
CC dsRNA.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC subfamily.
CC -!- SIMILARITY: Contains 2 DRBM (double-stranded RNA-binding) domains.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DHX9ID702ch1q25.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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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; CAH71701.1; -; Genomic_DNA.
DR EMBL; AL662837; CAH71701.1; JOINED; Genomic_DNA.
DR EMBL; AL662837; CAI19277.1; -; Genomic_DNA.
DR EMBL; AL355999; CAI19277.1; JOINED; 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 RefSeq; NP_001348.2; NM_001357.4.
DR UniGene; Hs.191518; -.
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 ProteinModelPortal; Q08211; -.
DR SMR; Q08211; 1-86, 169-263, 329-1071.
DR DIP; DIP-31504N; -.
DR IntAct; Q08211; 47.
DR MINT; MINT-5000572; -.
DR STRING; 9606.ENSP00000356520; -.
DR PhosphoSite; Q08211; -.
DR DMDM; 116241330; -.
DR SWISS-2DPAGE; Q08211; -.
DR PaxDb; Q08211; -.
DR PRIDE; Q08211; -.
DR Ensembl; ENST00000367549; ENSP00000356520; ENSG00000135829.
DR GeneID; 1660; -.
DR KEGG; hsa:1660; -.
DR UCSC; uc001gpr.3; human.
DR CTD; 1660; -.
DR GeneCards; GC01P182808; -.
DR H-InvDB; HIX0001404; -.
DR H-InvDB; HIX0149309; -.
DR HGNC; HGNC:2750; DHX9.
DR HPA; CAB011819; -.
DR HPA; HPA028050; -.
DR MIM; 603115; gene.
DR neXtProt; NX_Q08211; -.
DR PharmGKB; PA27232; -.
DR eggNOG; COG1643; -.
DR HOGENOM; HOG000247063; -.
DR HOVERGEN; HBG039429; -.
DR InParanoid; Q08211; -.
DR KO; K13184; -.
DR OMA; VDDWIRL; -.
DR OrthoDB; EOG76471V; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RNA_Helicase_A; -.
DR GenomeRNAi; 1660; -.
DR NextBio; 6832; -.
DR PMAP-CutDB; Q08211; -.
DR PRO; PR:Q08211; -.
DR Bgee; Q08211; -.
DR CleanEx; HS_DHX9; -.
DR Genevestigator; Q08211; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc.
DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; TAS:ProtInc.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
DR GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
DR Gene3D; 3.30.160.20; -; 2.
DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014720; dsRNA-bd_dom.
DR InterPro; IPR011709; DUF1605.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Helicase; Hydrolase; Methylation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1 1270 ATP-dependent RNA helicase A.
FT /FTId=PRO_0000055157.
FT DOMAIN 3 71 DRBM 1.
FT DOMAIN 180 252 DRBM 2.
FT DOMAIN 398 564 Helicase ATP-binding.
FT DOMAIN 636 809 Helicase C-terminal.
FT NP_BIND 411 419 ATP.
FT REGION 1 250 Interaction with CREBBP.
FT REGION 230 325 Interaction with BRCA1.
FT REGION 331 380 MTAD.
FT REGION 1151 1260 NTD.
FT MOTIF 511 514 DEIH box.
FT MOTIF 586 595 Nuclear localization signal (Potential).
FT MOD_RES 87 87 Phosphoserine.
FT MOD_RES 191 191 N6-acetyllysine.
FT MOD_RES 199 199 N6-acetyllysine.
FT MOD_RES 321 321 Phosphoserine.
FT MOD_RES 1024 1024 N6-acetyllysine.
FT VAR_SEQ 1 1035 Missing (in isoform 2).
FT /FTId=VSP_042314.
FT VARIANT 894 894 I -> V (in dbSNP:rs1049264).
FT /FTId=VAR_052179.
FT MUTAGEN 332 332 W->A: Abrogates transcriptional
FT activation by the MTAD domain.
FT MUTAGEN 339 339 W->A: Abrogates transcriptional
FT activation and RNA polymerase II binding
FT by the MTAD domain.
FT MUTAGEN 342 342 W->A: Abrogates transcriptional
FT activation by the MTAD domain.
FT MUTAGEN 417 417 K->R: Abrogates transcriptional
FT activation.
FT MUTAGEN 1163 1163 Missing: Abolishes nuclear localization.
FT MUTAGEN 1166 1166 R->L: Abolishes nuclear localization.
FT MUTAGEN 1166 1166 Missing: Abolishes nuclear localization.
FT CONFLICT 20 20 S -> T (in Ref. 1; AAB48855).
FT CONFLICT 108 109 TM -> HH (in Ref. 1; AAB48855).
FT CONFLICT 114 116 PPH -> LHI (in Ref. 1; AAB48855).
FT CONFLICT 186 186 N -> I (in Ref. 1; AAB48855).
FT CONFLICT 260 260 S -> T (in Ref. 1; AAB48855).
FT CONFLICT 478 478 I -> V (in Ref. 1; AAB48855).
FT CONFLICT 521 521 D -> S (in Ref. 1; AAB48855).
FT CONFLICT 541 541 L -> F (in Ref. 1; AAB48855).
FT CONFLICT 560 565 IIEVYG -> SLKLW (in Ref. 1; AAB48855).
FT CONFLICT 590 590 D -> K (in Ref. 5; AAH25245).
FT CONFLICT 749 749 A -> S (in Ref. 1; AAB48855 and 3;
FT CAA71668).
FT CONFLICT 768 770 VRP -> STA (in Ref. 1; AAB48855 and 3;
FT CAA71668).
FT CONFLICT 828 828 A -> G (in Ref. 5; AAI07882).
FT CONFLICT 899 899 R -> Q (in Ref. 1; AAB48855).
FT CONFLICT 1037 1037 K -> N (in Ref. 1; AAB48855).
FT CONFLICT 1063 1063 T -> P (in Ref. 1; AAB48855 and 3;
FT CAA71668).
FT CONFLICT 1140 1140 R -> E (in Ref. 1; AAB48855).
FT CONFLICT 1204 1211 NSFRAGYG -> TPSGRIC (in Ref. 1;
FT AAB48855).
FT CONFLICT 1261 1270 FGQGRGGGGY -> LDIEEEVAAIKLGYVSSVCRQ (in
FT Ref. 1; AAB48855).
FT HELIX 4 14
FT STRAND 20 28
FT STRAND 31 39
FT STRAND 47 53
FT HELIX 54 71
FT HELIX 77 79
FT HELIX 170 173
FT TURN 178 180
FT HELIX 181 191
FT STRAND 199 204
FT HELIX 206 208
FT STRAND 210 218
FT HELIX 220 222
FT STRAND 223 234
FT HELIX 235 252
FT TURN 341 344
FT TURN 351 354
FT HELIX 357 374
FT HELIX 376 386
FT HELIX 389 393
FT HELIX 394 403
FT STRAND 405 410
FT HELIX 417 431
FT HELIX 435 437
FT STRAND 439 446
FT HELIX 447 459
FT TURN 460 462
FT STRAND 467 473
FT STRAND 476 478
FT STRAND 482 490
FT HELIX 491 500
FT STRAND 507 510
FT HELIX 518 533
FT STRAND 537 543
FT HELIX 549 554
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
//
MIM
603115
*RECORD*
*FIELD* NO
603115
*FIELD* TI
*603115 DEAH BOX POLYPEPTIDE 9; DHX9
;;DEAD/H BOX 9; DDX9;;
RNA HELICASE A;;
NUCLEAR DNA HELICASE II; NDHII
read more*FIELD* TX
CLONING
RNA helicases play important roles in transcription, RNA processing,
translation, and RNA replication. DEAD box proteins are putative RNA
helicases that have a characteristic Asp-Glu-Ala-Asp (DEAD) box as 1 of
8 highly conserved sequence motifs. See 600396. The Drosophila
'maleless' (MLE) RNA helicase is thought to act as a regulator of
X-linked gene expression. Lee and Hurwitz (1992) isolated and
characterized human RNA helicase A, an abundant 130-kD nuclear enzyme of
HeLa cells that unwinds double-stranded RNA in a 3-prime to 5-prime
direction. By screening a HeLa cell expression library with antibodies
against RNA helicase A, Lee and Hurwitz (1993) identified cDNAs encoding
the enzyme. The predicted 1,279-amino acid protein shares sequence
homology with the Drosophila MLE protein and other members of the DEAH
subfamily of RNA helicases. The amino acid sequences of MLE and RNA
helicase A are 49% identical, and antibodies against MLE recognize RNA
helicase A. Northern blot analysis of HeLa cell RNA revealed RNA
helicase A expression as a 4.2-kb transcript. Lee et al. (1998) isolated
mouse RNA helicase A cDNAs. The predicted mouse and human proteins share
87% identity.
Zhang et al. (1995) identified bovine nuclear DNA helicase II (NDHII) as
the homolog of human RNA helicase A. Bovine NDHII unwinds both DNA and
RNA. Zhang and Grosse (1997) demonstrated that recombinant human RNA
helicase A, or NDHII, also unwinds both double-stranded RNA and
double-stranded DNA in an ATP-dependent manner. They reported that the
protein contains 2 copies of a double-stranded RNA-binding domain at its
N terminus, a DEIH helicase core, and a C-terminal RGG box nucleic
acid-binding domain. By analysis of mutant proteins, Zhang and Grosse
(1997) found that the RNA-binding domains and RGG box influence and
regulate RNA helicase A activity. They suggested a model in which RNA
helicase A participates in melting of DNA:RNA hybrids, such as those
that occur during transcription.
Leukophysin (LKP) is a 28-kD protein present in granulated CD8 (see
186910)-positive and CD4 (186940)-positive cytotoxic T lymphocytes and
in the U937 monocytic cell line. By immunoscreening a U937 cDNA library,
Abdelhaleem et al. (1996) obtained a cDNA encoding LKP.
Immunofluorescence microscopy demonstrated the presence of LKP in
granzyme A (140050)-negative granules. The deduced 235-amino acid
protein contains multiple N-myristoylation sites, a potential N-linked
glycosylation site, a potential O-linked glycosylation site, and 6
potential phosphorylation sites. LKP lacks typical RNA-binding domains
but is identical to the C terminus of DDX9. Abdelhaleem et al. (1996)
concluded that LKP is a component of granule membranes and is most
likely a splice variant of DDX9.
GENE FUNCTION
Using an affinity purification approach, Robb and Rana (2007) found that
RHA associated with small interfering RNA (siRNA), AGO2 (EIF2C2;
606229), TRBP (TARBP2; 605053), and DICER (606241) in the RNA-induced
silencing complex (RISC) in human cell lines. RHA specifically
interacted with active RISC, and depletion of RHA in cells before
programming with siRNA or short hairpin RNA reduced gene silencing due
to decreased RISC formation. RHA depletion also reduced recruitment of
siRNA to intracellular AGO2, supporting a role for RHA in RISC loading.
MAPPING
Lee et al. (1998) stated that the RNA helicase A gene maps to human
chromosome 1q25. By analysis of an interspecific backcross, they mapped
the mouse homolog to chromosome 1, in a region showing homology of
synteny with human chromosome 1q.
*FIELD* RF
1. 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. Immun. 156: 2026-2035, 1996.
2. Lee, C.-G.; Eki, T.; Okumura, K.; da Costa Soares, V.; Hurwitz,
J.: Molecular analysis of the cDNA and genomic DNA encoding mouse
RNA helicase A. Genomics 47: 365-371, 1998.
3. Lee, C.-G.; Hurwitz, J.: Human RNA helicase A is homologous to
the maleless protein of Drosophila. J. Biol. Chem. 268: 16822-16830,
1993.
4. Lee, C. G.; Hurwitz, J.: A new RNA helicase isolated from HeLa
cells that catalytically translocates in the 3-prime to 5-prime direction. J.
Biol. Chem. 267: 4398-4407, 1992.
5. Robb, G. B.; Rana, T. M.: RNA helicase A interacts with RISC in
human cells and functions in RISC loading. Molec. Cell 26: 523-537,
2007.
6. Zhang, S.; Grosse, F.: Domain structure of human nuclear DNA helicase
II (RNA helicase A). J. Biol. Chem. 272: 11487-11494, 1997.
7. Zhang, S.; Maacke, H.; Grosse, F.: Molecular cloning of the gene
encoding nuclear DNA helicase II: a bovine homologue of human RNA
helicase A and Drosophila Mle protein. J. Biol. Chem. 270: 16422-16427,
1995.
*FIELD* CN
Patricia A. Hartz - updated: 7/9/2007
Paul J. Converse - updated: 8/27/2001
*FIELD* CD
Rebekah S. Rasooly: 10/12/1998
*FIELD* ED
wwang: 03/30/2010
wwang: 3/30/2010
mgross: 9/27/2007
terry: 7/9/2007
mgross: 8/27/2001
alopez: 11/19/1998
alopez: 10/15/1998
alopez: 10/12/1998
*RECORD*
*FIELD* NO
603115
*FIELD* TI
*603115 DEAH BOX POLYPEPTIDE 9; DHX9
;;DEAD/H BOX 9; DDX9;;
RNA HELICASE A;;
NUCLEAR DNA HELICASE II; NDHII
read more*FIELD* TX
CLONING
RNA helicases play important roles in transcription, RNA processing,
translation, and RNA replication. DEAD box proteins are putative RNA
helicases that have a characteristic Asp-Glu-Ala-Asp (DEAD) box as 1 of
8 highly conserved sequence motifs. See 600396. The Drosophila
'maleless' (MLE) RNA helicase is thought to act as a regulator of
X-linked gene expression. Lee and Hurwitz (1992) isolated and
characterized human RNA helicase A, an abundant 130-kD nuclear enzyme of
HeLa cells that unwinds double-stranded RNA in a 3-prime to 5-prime
direction. By screening a HeLa cell expression library with antibodies
against RNA helicase A, Lee and Hurwitz (1993) identified cDNAs encoding
the enzyme. The predicted 1,279-amino acid protein shares sequence
homology with the Drosophila MLE protein and other members of the DEAH
subfamily of RNA helicases. The amino acid sequences of MLE and RNA
helicase A are 49% identical, and antibodies against MLE recognize RNA
helicase A. Northern blot analysis of HeLa cell RNA revealed RNA
helicase A expression as a 4.2-kb transcript. Lee et al. (1998) isolated
mouse RNA helicase A cDNAs. The predicted mouse and human proteins share
87% identity.
Zhang et al. (1995) identified bovine nuclear DNA helicase II (NDHII) as
the homolog of human RNA helicase A. Bovine NDHII unwinds both DNA and
RNA. Zhang and Grosse (1997) demonstrated that recombinant human RNA
helicase A, or NDHII, also unwinds both double-stranded RNA and
double-stranded DNA in an ATP-dependent manner. They reported that the
protein contains 2 copies of a double-stranded RNA-binding domain at its
N terminus, a DEIH helicase core, and a C-terminal RGG box nucleic
acid-binding domain. By analysis of mutant proteins, Zhang and Grosse
(1997) found that the RNA-binding domains and RGG box influence and
regulate RNA helicase A activity. They suggested a model in which RNA
helicase A participates in melting of DNA:RNA hybrids, such as those
that occur during transcription.
Leukophysin (LKP) is a 28-kD protein present in granulated CD8 (see
186910)-positive and CD4 (186940)-positive cytotoxic T lymphocytes and
in the U937 monocytic cell line. By immunoscreening a U937 cDNA library,
Abdelhaleem et al. (1996) obtained a cDNA encoding LKP.
Immunofluorescence microscopy demonstrated the presence of LKP in
granzyme A (140050)-negative granules. The deduced 235-amino acid
protein contains multiple N-myristoylation sites, a potential N-linked
glycosylation site, a potential O-linked glycosylation site, and 6
potential phosphorylation sites. LKP lacks typical RNA-binding domains
but is identical to the C terminus of DDX9. Abdelhaleem et al. (1996)
concluded that LKP is a component of granule membranes and is most
likely a splice variant of DDX9.
GENE FUNCTION
Using an affinity purification approach, Robb and Rana (2007) found that
RHA associated with small interfering RNA (siRNA), AGO2 (EIF2C2;
606229), TRBP (TARBP2; 605053), and DICER (606241) in the RNA-induced
silencing complex (RISC) in human cell lines. RHA specifically
interacted with active RISC, and depletion of RHA in cells before
programming with siRNA or short hairpin RNA reduced gene silencing due
to decreased RISC formation. RHA depletion also reduced recruitment of
siRNA to intracellular AGO2, supporting a role for RHA in RISC loading.
MAPPING
Lee et al. (1998) stated that the RNA helicase A gene maps to human
chromosome 1q25. By analysis of an interspecific backcross, they mapped
the mouse homolog to chromosome 1, in a region showing homology of
synteny with human chromosome 1q.
*FIELD* RF
1. 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. Immun. 156: 2026-2035, 1996.
2. Lee, C.-G.; Eki, T.; Okumura, K.; da Costa Soares, V.; Hurwitz,
J.: Molecular analysis of the cDNA and genomic DNA encoding mouse
RNA helicase A. Genomics 47: 365-371, 1998.
3. Lee, C.-G.; Hurwitz, J.: Human RNA helicase A is homologous to
the maleless protein of Drosophila. J. Biol. Chem. 268: 16822-16830,
1993.
4. Lee, C. G.; Hurwitz, J.: A new RNA helicase isolated from HeLa
cells that catalytically translocates in the 3-prime to 5-prime direction. J.
Biol. Chem. 267: 4398-4407, 1992.
5. Robb, G. B.; Rana, T. M.: RNA helicase A interacts with RISC in
human cells and functions in RISC loading. Molec. Cell 26: 523-537,
2007.
6. Zhang, S.; Grosse, F.: Domain structure of human nuclear DNA helicase
II (RNA helicase A). J. Biol. Chem. 272: 11487-11494, 1997.
7. Zhang, S.; Maacke, H.; Grosse, F.: Molecular cloning of the gene
encoding nuclear DNA helicase II: a bovine homologue of human RNA
helicase A and Drosophila Mle protein. J. Biol. Chem. 270: 16422-16427,
1995.
*FIELD* CN
Patricia A. Hartz - updated: 7/9/2007
Paul J. Converse - updated: 8/27/2001
*FIELD* CD
Rebekah S. Rasooly: 10/12/1998
*FIELD* ED
wwang: 03/30/2010
wwang: 3/30/2010
mgross: 9/27/2007
terry: 7/9/2007
mgross: 8/27/2001
alopez: 11/19/1998
alopez: 10/15/1998
alopez: 10/12/1998