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ATP-dependent RNA helicase A (EC 3.6.4.13) (DEAH box protein 9) (mHEL-5) (Nuclear DNA helicase II) (NDH II) (RNA helicase A) (RHA)

 DHX9_MOUSE              Reviewed;        1380 AA.
O70133; O35931; O54703; Q5FWY1; Q6R5F7; Q9CSA2;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 2.
05-DEC-2018, entry version 171.
RecName: Full=ATP-dependent RNA helicase A {ECO:0000250|UniProtKB:Q08211};
EC=3.6.4.13 {ECO:0000250|UniProtKB:Q08211};
AltName: Full=DEAH box protein 9 {ECO:0000303|Ref.5};
Short=mHEL-5 {ECO:0000303|Ref.5};
AltName: Full=Nuclear DNA helicase II {ECO:0000250|UniProtKB:Q08211};
Short=NDH II {ECO:0000250|UniProtKB:Q08211};
AltName: Full=RNA helicase A {ECO:0000303|PubMed:9480750};
Short=RHA {ECO:0000303|PubMed:9480750};
Name=Dhx9 {ECO:0000312|MGI:MGI:108177};
Synonyms=Ddx9 {ECO:0000250|UniProtKB:Q08211};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
[GENOMIC DNA] OF 1-161.
STRAIN=129/Sv;
PubMed=9480750; DOI=10.1006/geno.1997.5139;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-756 (ISOFORM 3).
STRAIN=C57BL/6NCr;
PubMed=14691545; DOI=10.1371/journal.pbio.0000074;
Sharov A.A., Piao Y., Matoba R., Dudekula D.B., Qian Y., VanBuren V.,
Falco G., Martin P.R., Stagg C.A., Bassey U.C., Wang Y., Carter M.G.,
Hamatani T., Aiba K., Akutsu H., Sharova L., Tanaka T.S., Kimber W.L.,
Yoshikawa T., Jaradat S.A., Pantano S., Nagaraja R., Boheler K.R.,
Taub D., Hodes R.J., Longo D.L., Schlessinger D., Keller J., Klotz E.,
Kelsoe G., Umezawa A., Vescovi A.L., Rossant J., Kunath T.,
Hogan B.L.M., Curci A., D'Urso M., Kelso J., Hide W., Ko M.S.H.;
"Transcriptome analysis of mouse stem cells and early embryos.";
PLoS Biol. 1:410-419(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-756 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-264 (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE OF 386-919 (ISOFORMS 1/2/3).
STRAIN=C57BL/6J;
Kisielow P., Miazek A.;
"mHEL-5.";
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[6]
SUBCELLULAR LOCATION.
PubMed=10413677;
Zhang S., Herrmann C., Grosse F.;
"Nucleolar localization of murine nuclear DNA helicase II (RNA
helicase A).";
J. Cell Sci. 112:2693-2703(1999).
[7]
INTERACTION WITH SP7, AND SUBCELLULAR LOCATION.
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).
[8]
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH EIF2AK2, AND
PHOSPHORYLATION.
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 2), AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
FUNCTION IN CIRCADIAN RHYTHMS, AND IDENTIFICATION IN A LARGE PER
COMPLEX.
PubMed=22767893; DOI=10.1126/science.1221592;
Padmanabhan K., Robles M.S., Westerling T., Weitz C.J.;
"Feedback regulation of transcriptional termination by the mammalian
circadian clock PERIOD complex.";
Science 337:599-602(2012).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[15]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1167; ARG-1312; ARG-1323;
ARG-1339; ARG-1346; ARG-1353; ARG-1361 AND ARG-1372, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
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).
[16]
FUNCTION, 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).
[17]
FUNCTION.
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).
[18]
STRUCTURE BY NMR OF 4-262.
RIKEN structural genomics initiative (RSGI);
"Solution structure of double-stranded RNA-binding motifs from
hypothetical protein BAB28848.";
Submitted (NOV-2004) to the PDB data bank.
[19]
INTERACTION WITH ZIC2.
PubMed=18068128; DOI=10.1016/j.febslet.2007.11.080;
Ishiguro A., Aruga J.;
"Functional role of Zic2 phosphorylation in transcriptional
regulation.";
FEBS Lett. 582:154-158(2008).
-!- 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. 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). 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. Binds dsDNA, single-stranded DNA (ssDNA),
dsRNA, ssRNA and poly(A)-containing RNA. 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. Plays a role in DNA replication at origins of
replication and cell cycle progression. 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. Binds to the CDKN2A
promoter. Plays several roles in post-transcriptional regulation
of gene expression. In cooperation with NUP98, promotes pre-mRNA
alternative splicing activities of a subset of genes (By
similarity). 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 (PubMed:22767893). 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. Component of the coding region determinant (CRD)-
mediated complex that promotes cytoplasmic MYC mRNA stability.
Plays a role in mRNA translation. Positively regulates translation
of selected mRNAs through its binding to post-transcriptional
control element (PCE) in the 5'-untranslated region (UTR).
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. Stimulates LIN28A-dependent
mRNA translation probably by facilitating ribonucleoprotein
remodeling during the process of translation. 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.
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 (By similarity).
{ECO:0000250|UniProtKB:Q08211, ECO:0000269|PubMed:22767893,
ECO:0000269|PubMed:28355180, ECO:0000269|PubMed:28636595}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
Evidence={ECO:0000250|UniProtKB:Q08211};
-!- SUBUNIT: Component of the coding region determinant (CRD)-mediated
complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1.
Identified in a mRNP complex, at least composed of DHX9, DDX3X,
ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2,
SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule
complex containing untranslated mRNAs (By similarity). The large
PER complex involved in the repression of transcriptional
termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1
and POLR2A (active) (PubMed:22767893). Associates (via DRBM
domains) with the RISC complex; this association occurs in a small
interfering (siRNA)-dependent manner. Associates with the SMN
complex; this association induces recruitment of DHX9 to the RNA
polymerase II. Associates with polysomes in a LIN28A-dependent
manner. Interacts (via C-terminus) with ACTB; this interaction is
direct and mediates the attachment to nuclear ribonucleoprotein
complexes (By similarity). 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. Interacts (via NTD domain) with
AKAP8L (via N-terminus). Interacts with BRCA1 (via C-terminus);
this interaction is direct and links BRCA1 to the RNA polymerase
II holoenzyme. Interacts (via N-terminus) with CREBBP; this
interaction mediates association with RNA polymerase II holoenzyme
and stimulates CREB-dependent transcriptional activation (By
similarity). 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.
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. Interacts with
HNRNPC; this interaction is direct, enhanced probably by their
concomitant binding to RNA and mediates the attachment to actin
filaments. Interacts (via NTD domain) with PRMT1. Interacts with
IGF2BP1. Interacts with IGF2BP2, IGF2BP3. Interacts (via DRBM
domains) with ILF3; this interaction occurs in a RNA-independent
manner. Interacts with Importin alpha/Importin beta receptor.
Interacts with LARP6 (via C-terminus); this interaction occurs in
a mRNA-independent manner. Interacts (via N- and C-terminus) with
LIN28A (via C-terminus); this interaction occurs in a RNA-
independent manner. Interacts with LMX1B. 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. Interacts with MBD2; this
interaction stimulates transcriptional activation in a CREB-
dependent manner. Interacts (via H2A and OB-fold regions) with
MYD88 (via TIR domain); this interaction is direct. Interacts with
NLRP9 upon rotavirus infection; this interaction may trigger NLRP9
inflammasome activation and inflammatory response. 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. 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. Interacts with RELA; this
interaction is direct and activates NF-kappa-B-mediated
transcription. Interacts (via MTAD region) with RNA polymerase II
holoenzyme; this interaction stimulates transcription activation
in a CREB-dependent manner. Interacts (via RGG region) with SMN1;
this interaction links SMN1 to the RNA polymerase II holoenzyme
(By similarity). 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. 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.
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. Interacts with XRCC5; this
interaction occurs in a RNA-dependent manner (By similarity).
Interacts with ZIC2 (via C2H2-type domain 3) (PubMed:17251188).
{ECO:0000250|UniProtKB:Q08211, ECO:0000269|PubMed:17251188,
ECO:0000269|PubMed:17303075, ECO:0000269|PubMed:19229320,
ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:28355180}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17303075}.
Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q08211}. Nucleus,
nucleolus {ECO:0000269|PubMed:10413677}. Cytoplasm
{ECO:0000250|UniProtKB:Q08211}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q08211}. Note=Nucleoplasmic shuttling
protein. Its nuclear import involves the nucleocytoplasmic
transport receptor Importin alpha/Importin beta receptor pathway
in a Ran-dependent manner. In interphase, localizes in nuclear
stress granules and at perichromatin fibrils and in cytoplasmic
ribonucleoprotein granules. Colocalizes with WRN and H2AFX at
centrosomes in a microtubule-dependent manner following DNA
damaging agent treatment. Excluded from the mitotic nucleus as
early as prophase and re-entered the nucleus at telophase.
Recruited in diffuse and discrete intranuclear foci (GLFG-body) in
a NUP98-dependent manner (By similarity). Colocalizes with SP7 in
the nucleus (PubMed:17303075). Colocalizes with ACTB at nuclear
actin filaments inside the nucleus or at the nuclear pore.
Colocalizes with HNRNPC at nuclear ribonucleoprotein complex
proteins in the nucleus. Localized in cytoplasmic mRNP granules
containing untranslated mRNAs (By similarity).
{ECO:0000250|UniProtKB:Q08211, ECO:0000269|PubMed:17303075}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O70133-1; Sequence=Displayed;
Name=2;
IsoId=O70133-2; Sequence=VSP_014779;
Note=Contains a phosphoserine at position 137.
{ECO:0000244|PubMed:17242355, ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:21183079};
Name=3;
IsoId=O70133-3; Sequence=VSP_014778;
-!- DOMAIN: DRBM domains cooperate for the binding to nucleic acid but
not for unwinding helicase activity. The helicase-associated
domain-2 (HA2) region is essential for the duplex RNA unwinding
helicase activity. The minimal transactivation region (MTAD)
mediates interaction with the RNA polymerase II holoenzyme and
stimulates transcriptional activation in a CREB-dependent manner.
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. 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. {ECO:0000250|UniProtKB:Q08211}.
-!- PTM: Methylated. PRMT1-mediated methylation of undefined Arg
residues in the nuclear transport domain (NTD) is required for
nuclear import of DHX9. {ECO:0000250|UniProtKB:Q08211}.
-!- PTM: Phosphorylated by PRKDC; phosphorylation occurs in a RNA-
dependent manner. Phosphorylated by EIF2AK2/PKR; this
phosphorylation reduces its association with double-stranded RNA.
{ECO:0000250|UniProtKB:Q08211}.
-!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH89159.1; Type=Frameshift; Positions=447, 448; Evidence={ECO:0000305};
Sequence=AAR87796.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; U91922; AAC05725.1; -; mRNA.
EMBL; AF023530; AAC05301.1; -; Genomic_DNA.
EMBL; AY512925; AAR87796.1; ALT_SEQ; mRNA.
EMBL; BC089159; AAH89159.1; ALT_SEQ; mRNA.
EMBL; AK013423; BAB28848.1; -; mRNA.
EMBL; U92080; AAB72087.1; -; mRNA.
RefSeq; NP_031868.2; NM_007842.2.
UniGene; Mm.20000; -.
PDB; 1UIL; NMR; -; A=163-262.
PDB; 1WHQ; NMR; -; A=4-89.
PDB; 2RS6; NMR; -; A=4-89.
PDB; 2RS7; NMR; -; A=163-262.
PDBsum; 1UIL; -.
PDBsum; 1WHQ; -.
PDBsum; 2RS6; -.
PDBsum; 2RS7; -.
ProteinModelPortal; O70133; -.
SMR; O70133; -.
BioGrid; 199088; 10.
ComplexPortal; CPX-1089; CRD-mediated mRNA stability complex.
IntAct; O70133; 11.
MINT; O70133; -.
STRING; 10090.ENSMUSP00000038135; -.
iPTMnet; O70133; -.
PhosphoSitePlus; O70133; -.
SwissPalm; O70133; -.
EPD; O70133; -.
MaxQB; O70133; -.
PaxDb; O70133; -.
PeptideAtlas; O70133; -.
PRIDE; O70133; -.
GeneID; 13211; -.
KEGG; mmu:13211; -.
CTD; 1660; -.
MGI; MGI:108177; Dhx9.
eggNOG; KOG0920; Eukaryota.
eggNOG; COG1643; LUCA.
HOGENOM; HOG000247063; -.
HOVERGEN; HBG039429; -.
InParanoid; O70133; -.
KO; K13184; -.
PhylomeDB; O70133; -.
ChiTaRS; Dhx9; mouse.
EvolutionaryTrace; O70133; -.
PRO; PR:O70133; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_DHX9; -.
GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISS:UniProtKB.
GO; GO:0035068; C:micro-ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
GO; GO:0097165; C:nuclear stress granule; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005726; C:perichromatin fibrils; ISS:UniProtKB.
GO; GO:0042788; C:polysomal ribosome; ISS:UniProtKB.
GO; GO:0005844; C:polysome; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; ISS:UniProtKB.
GO; GO:0033681; F:ATP-dependent 3'-5' DNA/RNA helicase activity; ISS:UniProtKB.
GO; GO:0034459; F:ATP-dependent 3'-5' RNA helicase activity; ISS:UniProtKB.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; ISS:UniProtKB.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; ISS:UniProtKB.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003688; F:DNA replication origin binding; ISS:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
GO; GO:0061676; F:importin-alpha family protein binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
GO; GO:0017111; F:nucleoside-triphosphatase activity; ISS:UniProtKB.
GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; ISS:UniProtKB.
GO; GO:1905538; F:polysome binding; ISS:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0001069; F:regulatory region RNA binding; IDA:UniProtKB.
GO; GO:1905172; F:RISC complex binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
GO; GO:0000993; F:RNA polymerase II complex binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
GO; GO:1990518; F:single-stranded DNA-dependent ATP-dependent 3'-5' DNA helicase activity; ISS:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
GO; GO:0035197; F:siRNA binding; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
GO; GO:0045142; F:triplex DNA binding; ISS:UniProtKB.
GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
GO; GO:0071360; P:cellular response to exogenous dsRNA; ISS:UniProtKB.
GO; GO:0034605; P:cellular response to heat; IDA:MGI.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
GO; GO:0007623; P:circadian rhythm; IMP:MGI.
GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISO:MGI.
GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
GO; GO:0039695; P:DNA-templated viral transcription; ISO:MGI.
GO; GO:0044806; P:G-quadruplex DNA unwinding; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISS:UniProtKB.
GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; ISS:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
GO; GO:2000637; P:positive regulation of gene silencing by miRNA; ISS:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; IMP:UniProtKB.
GO; GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB.
GO; GO:1902741; P:positive regulation of interferon-alpha secretion; ISS:UniProtKB.
GO; GO:0035549; P:positive regulation of interferon-beta secretion; ISS:UniProtKB.
GO; GO:0032741; P:positive regulation of interleukin-18 production; IMP:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:1905698; P:positive regulation of polysome binding; ISS:UniProtKB.
GO; GO:0060760; P:positive regulation of response to cytokine stimulus; ISS:UniProtKB.
GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; ISS:UniProtKB.
GO; GO:0050434; P:positive regulation of viral transcription; ISO:MGI.
GO; GO:1904973; P:positive regulation of viral translation; ISO:MGI.
GO; GO:1903608; P:protein localization to cytoplasmic stress granule; ISO:MGI.
GO; GO:0070269; P:pyroptosis; IMP:UniProtKB.
GO; GO:2000765; P:regulation of cytoplasmic translation; ISS:UniProtKB.
GO; GO:0050691; P:regulation of defense response to virus by host; IMP:UniProtKB.
GO; GO:0050684; P:regulation of mRNA processing; ISS:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0010501; P:RNA secondary structure unwinding; ISS:UniProtKB.
GO; GO:0070922; P:small RNA loading onto RISC; ISS:UniProtKB.
GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; ISS:UniProtKB.
CDD; cd00048; DSRM; 2.
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; 1.
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; DNA-binding; Helicase; Hydrolase; Immunity;
Inflammatory response; Innate immunity; Isopeptide bond;
Metal-binding; Methylation; mRNA processing; mRNA splicing;
mRNA transport; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
Transcription; Transcription regulation; Transcription termination;
Translation regulation; Transport; Ubl conjugation.
CHAIN 1 1380 ATP-dependent RNA helicase A.
/FTId=PRO_0000055158.
DOMAIN 3 71 DRBM 1. {ECO:0000250|UniProtKB:Q08211,
ECO:0000255|PROSITE-ProRule:PRU00266}.
DOMAIN 182 254 DRBM 2. {ECO:0000250|UniProtKB:Q08211,
ECO:0000255|PROSITE-ProRule:PRU00266}.
DOMAIN 400 566 Helicase ATP-binding.
{ECO:0000250|UniProtKB:Q08211,
ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 638 811 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 413 421 ATP. {ECO:0000250|UniProtKB:Q08211,
ECO:0000255|PROSITE-ProRule:PRU00541}.
REGION 1 252 Interaction with CREBBP.
{ECO:0000250|UniProtKB:Q08211}.
REGION 5 9 siRNA-binding.
{ECO:0000250|UniProtKB:Q08211}.
REGION 53 55 siRNA-binding.
{ECO:0000250|UniProtKB:Q08211}.
REGION 184 188 siRNA-binding.
{ECO:0000250|UniProtKB:Q08211}.
REGION 232 327 Interaction with BRCA1.
{ECO:0000250|UniProtKB:Q08211}.
REGION 236 238 siRNA-binding.
{ECO:0000250|UniProtKB:Q08211}.
REGION 257 666 Necessary for interaction with RNA
polymerase II holoenzyme.
{ECO:0000250|UniProtKB:Q08211}.
REGION 315 954 Necessary for interaction with H2AFX.
{ECO:0000250|UniProtKB:Q08211}.
REGION 333 382 MTAD. {ECO:0000250|UniProtKB:Q08211}.
REGION 400 811 Core helicase.
{ECO:0000250|UniProtKB:Q08211}.
REGION 833 921 HA2. {ECO:0000250|UniProtKB:Q08211}.
REGION 960 1076 OB-fold. {ECO:0000250|UniProtKB:Q08211}.
REGION 1151 1366 NTD region.
{ECO:0000250|UniProtKB:Q08211}.
REGION 1152 1380 RGG. {ECO:0000250|UniProtKB:Q08211}.
MOTIF 513 516 DEAH box.
MOTIF 588 597 Nuclear localization signal (NLS1).
{ECO:0000255}.
MOTIF 1156 1174 Nuclear localization signal (NLS2).
{ECO:0000250|UniProtKB:Q08211}.
COMPBIAS 1171 1380 Arg/Gly/Ser/Tyr-rich.
METAL 420 420 Manganese.
{ECO:0000250|UniProtKB:Q08211}.
METAL 514 514 Manganese.
{ECO:0000250|UniProtKB:Q08211}.
MOD_RES 127 127 Phosphoserine.
{ECO:0000250|UniProtKB:Q08211}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 148 148 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 148 148 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:Q08211}.
MOD_RES 193 193 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q08211}.
MOD_RES 201 201 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q08211}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000250|UniProtKB:Q08211}.
MOD_RES 451 451 Phosphoserine.
{ECO:0000250|UniProtKB:Q08211}.
MOD_RES 508 508 Phosphoserine.
{ECO:0000250|UniProtKB:Q08211}.
MOD_RES 1026 1026 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q08211}.
MOD_RES 1167 1167 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1176 1176 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q08211}.
MOD_RES 1312 1312 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1323 1323 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1339 1339 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1346 1346 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1353 1353 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1361 1361 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1372 1372 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
CROSSLNK 699 699 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q08211}.
VAR_SEQ 1 216 Missing (in isoform 3).
{ECO:0000303|PubMed:14691545}.
/FTId=VSP_014778.
VAR_SEQ 123 123 E -> EA (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_014779.
CONFLICT 46 46 A -> R (in Ref. 1; AAC05725).
{ECO:0000305}.
CONFLICT 136 136 S -> A (in Ref. 1; AAC05725/AAC05301).
{ECO:0000305}.
CONFLICT 187 187 L -> V (in Ref. 2). {ECO:0000305}.
CONFLICT 189 189 Q -> H (in Ref. 1; AAC05725).
{ECO:0000305}.
CONFLICT 211 211 R -> G (in Ref. 4; BAB28848).
{ECO:0000305}.
CONFLICT 235 235 S -> C (in Ref. 1; AAC05725).
{ECO:0000305}.
CONFLICT 257 257 V -> C (in Ref. 1; AAC05725).
{ECO:0000305}.
CONFLICT 281 281 S -> P (in Ref. 1; AAC05725).
{ECO:0000305}.
CONFLICT 674 674 N -> M (in Ref. 5; AAB72087).
{ECO:0000305}.
CONFLICT 748 748 T -> I (in Ref. 5; AAB72087).
{ECO:0000305}.
CONFLICT 831 831 I -> V (in Ref. 5; AAB72087).
{ECO:0000305}.
HELIX 5 14 {ECO:0000244|PDB:1WHQ}.
STRAND 20 27 {ECO:0000244|PDB:1WHQ}.
STRAND 29 39 {ECO:0000244|PDB:1WHQ}.
STRAND 47 53 {ECO:0000244|PDB:1WHQ}.
HELIX 54 72 {ECO:0000244|PDB:1WHQ}.
TURN 77 79 {ECO:0000244|PDB:1WHQ}.
HELIX 172 175 {ECO:0000244|PDB:1UIL}.
HELIX 180 193 {ECO:0000244|PDB:1UIL}.
STRAND 201 206 {ECO:0000244|PDB:1UIL}.
STRAND 212 221 {ECO:0000244|PDB:1UIL}.
TURN 222 225 {ECO:0000244|PDB:1UIL}.
STRAND 226 231 {ECO:0000244|PDB:1UIL}.
HELIX 237 255 {ECO:0000244|PDB:1UIL}.
SEQUENCE 1380 AA; 149475 MW; 005D641CD9A4F0C9 CRC64;
MGDIKNFLYA WCGKRKMTPA YEIRAVGNKN RQKFMCEVRV EGFNYAGMGN STNKKDAQSN
AARDFVNYLV RINEVKSEEV PAVGIVPPPP ILSDTSDSTA SAAEGLPAPM GGPLPPHLAL
KAEENNSGVE SSGYGSPGPT WDRGANLKDY YSRKEEQEVQ ATLESEEVDL NAGLHGNWTL
ENAKARLNQY FQKEKIQGEY KYTQVGPDHN RSFIAEMTIY IKQLGRRIFA REHGSNKKLA
AQSCALSLVR QLYHLGVIEA YSGLTKKKEG ERVEPYKVFL SPDLELQLQN VVQELDLEIV
PPPVDPSMPV ILNIGKLAHF EPSQRQNAVG VVPWSPPQSN WNPWTSSNID EGPLAYASTE
QISMDLKNEL TYQMEQDHNL QSVLQERELL PVKKFEAEIL EAISSNSVVI IRGATGCGKT
TQVPQYILDD FIQNDRAAEC NIVVTQPRRI SAVAVAERVA YERGEEPGKS CGYSVRFESI
LPRPHASIMF CTVGVLLRKL EAGIRGISHV IVDEIHERDI NTDFLLVVLR DVVLAYPEVR
IVLMSATIDT TMFCEYFFNC PIIEVYGRTF PVQEYFLEDC IQMTQFIPPP KDKKKKDKED
DGGEDDDANC NLICGDEYGP ETKLSMSQLN EKETPFELIE ALLKYIETLN VPGAVLVFLP
GWNLIYTMQK HLENNSHFGS HRYQILPLHS QIPREEQRKV FDPVPDGVTK VILSTNIAET
SITINDVVYV IDSCKQKVKL FTAHNNMTNY ATVWASKTNL EQRKGRAGRV RPGFCFHLCS
RARFDRLETH MTPEMFRTPL HEIALSIKLL RLGGIGQFLA KAIEPPPLDA IIEAEHTLRE
LDALDANDEL TPLGRILAKL PIEPRFGKMM IMGCIFYVGD AVCTISAATC FPEPFISEGK
RLGYIHRNFA GNRFSDHVAL LSVFQAWDDA RMSGEEAEIR FCEQKRLNMA TLRMTWEAKV
QLKEILINSG FPEDCLLTQV FTNTGPDNNL DVVISLLAFG VYPNVCYHKE KRKILTTEGR
NALIHKSSVN CPFSSQDMKY PSPFFVFGEK IRTRAISAKG MTLVTPLQLL LFASKKVQSD
GQIVFIDDWI RLQISHEAAA CITIRAAMEA LVVEVSKQPN IISQLDPVNE HMLNTIRQIS
RPSAAGINLM IGSVRYGDGP RPPKMARYDN GSGYRRGYGG GGYGGGGYGG GYGSGGFGGG
FGSGGGFGGG FNSGGGGFGS GGGGFGSGGG GFGGGGGGFS GGGGGGFGGG RGGGGGGFGG
SGGFGNGGGG YGVGGGGYGG GGGGGYGGGS GGYGGGGYGG GEGYSISPNS YRGNYGGGGG
GYRGGSQGGY RNNFGGDYRG SSGDYRGSGG GYRGSGGFQR RGYGGGYFGQ GRGGGGGGGY


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GENTAUR GmbH
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Fax: (+49) 241 56 00 47 88

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Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
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GENTAUR Spain
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GENTAUR Poland Sp. z o.o.


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