DHX36_MOUSE
ID DHX36_MOUSE Reviewed; 1001 AA.
AC Q8VHK9; G3X8Y4; Q6ZPP7; Q9CSE8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=ATP-dependent DNA/RNA helicase DHX36 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9H2U1};
DE AltName: Full=DEAD/H box polypeptide 36 {ECO:0000303|PubMed:12198572};
DE AltName: Full=DEAH box protein 36 {ECO:0000305};
DE AltName: Full=MLE-like protein 1 {ECO:0000250|UniProtKB:Q9H2U1};
DE AltName: Full=RNA helicase associated with AU-rich element ARE {ECO:0000250|UniProtKB:Q9H2U1};
GN Name=Dhx36 {ECO:0000312|MGI:MGI:1919412};
GN Synonyms=Ddx36 {ECO:0000250|UniProtKB:Q9H2U1}, Kiaa1488,
GN Mlel1 {ECO:0000250|UniProtKB:Q9H2U1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=12198572;
RA Fu J.-J., Li L.-Y., Lu G.-X.;
RT "Molecular cloning and characterization of human DDX36 and mouse Ddx36
RT genes, new members of the DEAD/H box superfamily.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:655-661(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-422.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 321-1001.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, INTERACTION WITH TICAM1; DDX1 AND DDX21, IDENTIFICATION IN A
RP COMPLEX WITH DDX1; DDX21 AND TICAM1, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21703541; DOI=10.1016/j.immuni.2011.03.027;
RA Zhang Z., Kim T., Bao M., Facchinetti V., Jung S.Y., Ghaffari A.A., Qin J.,
RA Cheng G., Liu Y.J.;
RT "DDX1, DDX21, and DHX36 helicases form a complex with the adaptor molecule
RT TRIF to sense dsRNA in dendritic cells.";
RL Immunity 34:866-878(2011).
RN [9]
RP FUNCTION, INTERACTION WITH HDAC1 AND HDAC4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=21590736; DOI=10.1002/jbmr.426;
RA Kim H.N., Lee J.H., Bae S.C., Ryoo H.M., Kim H.H., Ha H., Lee Z.H.;
RT "Histone deacetylase inhibitor MS-275 stimulates bone formation in part by
RT enhancing Dhx36-mediated TNAP transcription.";
RL J. Bone Miner. Res. 26:2161-2173(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22422825; DOI=10.1182/blood-2011-08-362954;
RA Lai J.C., Ponti S., Pan D., Kohler H., Skoda R.C., Matthias P.,
RA Nagamine Y.;
RT "The DEAH-box helicase RHAU is an essential gene and critical for mouse
RT hematopoiesis.";
RL Blood 119:4291-4300(2012).
RN [11]
RP FUNCTION, G-QUADRUPLEX DNA-BINDING, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=25611385; DOI=10.1038/cddis.2014.571;
RA Gao X., Ma W., Nie J., Zhang C., Zhang J., Yao G., Han J., Xu J., Hu B.,
RA Du Y., Shi Q., Yang Z., Huang X., Zhang Y.;
RT "A G-quadruplex DNA structure resolvase, RHAU, is essential for
RT spermatogonia differentiation.";
RL Cell Death Dis. 6:E1610-E1610(2015).
RN [12]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=26489465; DOI=10.1016/j.celrep.2015.09.043;
RA Nie J., Jiang M., Zhang X., Tang H., Jin H., Huang X., Yuan B., Zhang C.,
RA Lai J.C., Nagamine Y., Pan D., Wang W., Yang Z.;
RT "Post-transcriptional Regulation of Nkx2-5 by RHAU in Heart Development.";
RL Cell Rep. 13:723-732(2015).
CC -!- FUNCTION: Multifunctional ATP-dependent helicase that unwinds G-
CC quadruplex (G4) structures (PubMed:25611385). Plays a role in many
CC biological processes such as genomic integrity, gene expression
CC regulations and as a sensor to initiate antiviral responses
CC (PubMed:21703541, PubMed:21590736). G4 structures correspond to helical
CC structures containing guanine tetrads (By similarity). Binds with high
CC affinity to and unwinds G4 structures that are formed in nucleic acids
CC (G4-ADN and G4-RNA) (By similarity). Plays a role in genomic integrity
CC (By similarity). Converts the G4-RNA structure present in telomerase
CC RNA template component (TREC) into a double-stranded RNA to promote P1
CC helix formation that acts as a template boundary ensuring accurate
CC reverse transcription (By similarity). Plays a role in transcriptional
CC regulation. Resolves G4-DNA structures in promoters of genes, such as
CC YY1, KIT/c-kit and ALPL and positively regulates their expression
CC (PubMed:25611385) (By similarity). Plays a role in post-transcriptional
CC regulation (By similarity). Unwinds a G4-RNA structure located in the
CC 3'-UTR polyadenylation site of the pre-mRNA TP53 and stimulates TP53
CC pre-mRNA 3'-end processing in response to ultraviolet (UV)-induced DNA
CC damage (By similarity). Binds to the precursor-microRNA-134 (pre-miR-
CC 134) terminal loop and regulates its transport into the synapto-
CC dendritic compartment (By similarity). Involved in the pre-miR-134-
CC dependent inhibition of target gene expression and the control of
CC dendritic spine size (By similarity). Plays a role in the regulation of
CC cytoplasmic mRNA translation and mRNA stability (By similarity). Binds
CC to both G4-RNA structures and alternative non-quadruplex-forming
CC sequence within the 3'-UTR of the PITX1 mRNA regulating negatively
CC PITX1 protein expression (By similarity). Binds to both G4-RNA
CC structure in the 5'-UTR and AU-rich elements (AREs) localized in the
CC 3'-UTR of NKX2-5 mRNA to either stimulate protein translation or induce
CC mRNA decay in an ELAVL1-dependent manner, respectively (By similarity).
CC Binds also to ARE sequences present in several mRNAs mediating exosome-
CC mediated 3'-5' mRNA degradation (By similarity). Involved in
CC cytoplasmic urokinase-type plasminogen activator (uPA) mRNA decay (By
CC similarity). Component of a multi-helicase-TICAM1 complex that acts as
CC a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a
CC role in the activation of a cascade of antiviral responses including
CC the induction of pro-inflammatory cytokines via the adapter molecule
CC TICAM1 (PubMed:21703541). Required for the early embryonic development
CC and hematopoiesis (PubMed:22422825). Involved in the regulation of
CC cardioblast differentiation and proliferation during heart development
CC (PubMed:26489465). Involved in spermatogonia differentiation
CC (PubMed:25611385). May play a role in ossification (PubMed:21590736).
CC {ECO:0000250|UniProtKB:D4A2Z8, ECO:0000250|UniProtKB:Q05B79,
CC ECO:0000250|UniProtKB:Q9H2U1, ECO:0000269|PubMed:21590736,
CC ECO:0000269|PubMed:21703541, ECO:0000269|PubMed:22422825,
CC ECO:0000269|PubMed:25611385, ECO:0000269|PubMed:26489465}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:Q9H2U1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q05B79};
CC -!- ACTIVITY REGULATION: ATPase activity is enhanced in the presence of
CC homomeric poly(U) RNAs, but not by double-stranded DNA (dsDNA), double-
CC stranded RNA (dsRNA) and tRNA. {ECO:0000250|UniProtKB:Q9H2U1}.
CC -!- SUBUNIT: Found in a multi-helicase-TICAM1 complex at least composed of
CC DHX36, DDX1, DDX21 and TICAM1; this complex exists in resting cells
CC with or without dsRNA poly(I:C) ligand stimulation (PubMed:21703541).
CC Interacts (via C-terminus) with TICAM1 (via TIR domain)
CC (PubMed:21703541). Interacts (via C-terminus) with DDX21; this
CC interaction serves as bridges to TICAM1 (PubMed:21703541). Interacts
CC with TERT; this interaction is dependent on the ability of DHX36 to
CC bind to the G-quadruplex RNA (G4-RNA) structure present in the
CC telomerase RNA template component (TERC). Interacts with DKC1; this
CC interaction is dependent on the ability of DHX36 to bind to the G4-RNA
CC structure present in TERC. Interacts with PARN; this interaction
CC stimulates PARN to enhance uPA mRNA decay. Interacts with EXOSC3; this
CC interaction occurs in a RNase-insensitive manner. Interacts with
CC EXOSC10; this interaction occurs in a RNase-insensitive manner.
CC Interacts with ILF3; this interaction occurs in a RNA-dependent manner.
CC Interacts with ELAVL1; this interaction occurs in an RNA-dependent
CC manner. Interacts with DDX5; this interaction occurs in a RNA-dependent
CC manner. Interacts with DDX17; this interaction occurs in a RNA-
CC dependent manner. Interacts with HDAC1; this interaction occurs in a
CC RNA-dependent manner (By similarity) (PubMed:21590736). Interacts with
CC HDAC3; this interaction occurs in a RNA-dependent manner (By
CC similarity). Interacts with HDAC4 (PubMed:21590736). Interacts with
CC AGO1. Interacts with AGO2 (By similarity). Interacts with ERCC6 (By
CC similarity). {ECO:0000250|UniProtKB:Q9H2U1,
CC ECO:0000269|PubMed:21590736, ECO:0000269|PubMed:21703541}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H2U1}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9H2U1}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:21703541}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q9H2U1}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q9H2U1}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q9H2U1}. Mitochondrion
CC {ECO:0000269|PubMed:21703541}. Perikaryon
CC {ECO:0000250|UniProtKB:D4A2Z8}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:D4A2Z8}. Cell projection, axon
CC {ECO:0000250|UniProtKB:D4A2Z8}. Note=Predominantly localized in the
CC nucleus. Colocalizes with SRSF2 in nuclear speckles. Colocalizes with
CC DDX5 in nucleolar caps upon transcription inhibition. Accumulates and
CC colocalized with TIA1 in cytoplasmic stress granules (SGs) in an
CC arsenite-, heat shock- and RNA-binding-dependent manner. Shuttles into
CC and out of SGs in an ATPase-dependent manner (By similarity).
CC Colocalizes in the cytosol with the multi-helicase-TICAM1 complex that
CC translocates to the mitochondria upon poly(I:C) stimulation
CC (PubMed:21703541). {ECO:0000250|UniProtKB:Q9H2U1,
CC ECO:0000269|PubMed:21703541}.
CC -!- TISSUE SPECIFICITY: Expressed in spermatogonia stem cells and primary
CC spermatocytes (at protein level) (PubMed:25611385). Expressed strongly
CC in testis. Weakly expressed in heart, lung, liver, kidney, small
CC intestine, spleen, lymphe node and thymus (PubMed:25611385).
CC {ECO:0000269|PubMed:25611385}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryonic heart at 10.5 and
CC increases from 14.5 to 16.5 dpc, and then gradually decreases until
CC postnal day 7 (PubMed:26489465). Expressed during the testicular
CC development from embryonic day 18.5 to postnatal day 35
CC (PubMed:25611385). {ECO:0000269|PubMed:25611385,
CC ECO:0000269|PubMed:26489465}.
CC -!- DOMAIN: The DHX36-specific motif (DSM) form folds into a DNA-binding-
CC induced alpha-helix that together with the oligonucleotide and
CC oligosaccharide-binding-fold-like (OB-fold-like) subdomain bind to Myc-
CC promoter G4-DNA-containing structure in an ATP-dependent manner. Upon
CC G4-DNA-binding, DHX36 pulls on DSM in the 3'-direction, inducing
CC rearrangement of the RecA-like 1 and 2 and the degenerate-winged-helix
CC (WH) regions; these rearrangements are propbably responsible for the
CC ATP-independent repetitive G4-DNA unfolding activity, one residue at a
CC time. Upon resolving of G4-DNA into separate nucleotide strands, and
CC ATP hydrolysis, the apoprotein of DHX36 seems incompatible with G4-DNA-
CC binding (By similarity). The N-terminus is necessary for its
CC recruitment to cytoplasmic stress granules (SGs) upon arsenite-induced
CC treatment (By similarity). {ECO:0000250|UniProtKB:Q05B79,
CC ECO:0000250|UniProtKB:Q9H2U1}.
CC -!- DISRUPTION PHENOTYPE: Mice die at around embryonic 7 days post-coitum
CC (dpc). Conditional knockout mice in the hematopoeitic system leads to
CC hemolytic anemia, a reduction in blood platelet and erythroblast
CC development (PubMed:22422825). Cardiac progenitor-cell-specific
CC knockout mice die around 12.5 dpc and lead to abnormal cardiovascular
CC development with a reduction in cardiomyocyte proliferation. Mice
CC display increased NKX2-5 mRNA but decreased NKX2-5 protein levels,
CC respectively, in the heart at 12.5 dpc compared to wild-type mice
CC (PubMed:26489465). Male germ-cell-specific knockout mice lead to
CC testicular hypoplasia development, due to spermatogonia differentiation
CC block, meiosis initiation arrest as early as meiosis I stage and an
CC absence of mature sperm in the epididymis (PubMed:25611385). Mice show
CC several alteration in meiosis-related gene expression such as the
CC differentiating spermatogonia markers KIT/c-kit (PubMed:25611385).
CC {ECO:0000269|PubMed:22422825, ECO:0000269|PubMed:25611385,
CC ECO:0000269|PubMed:26489465}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; AF448804; AAL47006.1; -; mRNA.
DR EMBL; AC114424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466530; EDL35384.1; -; Genomic_DNA.
DR EMBL; AK129373; BAC98183.1; -; mRNA.
DR EMBL; AK013031; BAB28610.1; -; mRNA.
DR CCDS; CCDS17379.1; -.
DR RefSeq; NP_082412.2; NM_028136.2.
DR RefSeq; XP_011238540.1; XM_011240238.1.
DR PDB; 6UP2; X-ray; 1.97 A; A=153-982.
DR PDB; 6UP3; X-ray; 2.69 A; A=153-982.
DR PDB; 6UP4; X-ray; 2.40 A; A=153-982.
DR PDBsum; 6UP2; -.
DR PDBsum; 6UP3; -.
DR PDBsum; 6UP4; -.
DR AlphaFoldDB; Q8VHK9; -.
DR SMR; Q8VHK9; -.
DR BioGRID; 215193; 10.
DR DIP; DIP-48576N; -.
DR IntAct; Q8VHK9; 3.
DR STRING; 10090.ENSMUSP00000029336; -.
DR iPTMnet; Q8VHK9; -.
DR PhosphoSitePlus; Q8VHK9; -.
DR EPD; Q8VHK9; -.
DR MaxQB; Q8VHK9; -.
DR PaxDb; Q8VHK9; -.
DR PeptideAtlas; Q8VHK9; -.
DR PRIDE; Q8VHK9; -.
DR ProteomicsDB; 279655; -.
DR Antibodypedia; 33625; 182 antibodies from 27 providers.
DR DNASU; 72162; -.
DR Ensembl; ENSMUST00000029336; ENSMUSP00000029336; ENSMUSG00000027770.
DR GeneID; 72162; -.
DR KEGG; mmu:72162; -.
DR UCSC; uc008pjn.2; mouse.
DR CTD; 170506; -.
DR MGI; MGI:1919412; Dhx36.
DR VEuPathDB; HostDB:ENSMUSG00000027770; -.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000156903; -.
DR HOGENOM; CLU_001832_1_4_1; -.
DR InParanoid; Q8VHK9; -.
DR OMA; GKMILMS; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; Q8VHK9; -.
DR TreeFam; TF324744; -.
DR Reactome; R-MMU-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR BioGRID-ORCS; 72162; 32 hits in 79 CRISPR screens.
DR ChiTaRS; Dhx36; mouse.
DR PRO; PR:Q8VHK9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8VHK9; protein.
DR Bgee; ENSMUSG00000027770; Expressed in ventromedial nucleus of hypothalamus and 256 other tissues.
DR Genevisible; Q8VHK9; MM.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IMP:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IDA:UniProtKB.
DR GO; GO:0002151; F:G-quadruplex RNA binding; ISS:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISS:UniProtKB.
DR GO; GO:0070883; F:pre-miRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0070034; F:telomerase RNA binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:1903843; P:cellular response to arsenite ion; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0001503; P:ossification; IMP:UniProtKB.
DR GO; GO:0051891; P:positive regulation of cardioblast differentiation; IMP:UniProtKB.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1901534; P:positive regulation of hematopoietic progenitor cell differentiation; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISO:MGI.
DR GO; GO:1904582; P:positive regulation of intracellular mRNA localization; ISS:UniProtKB.
DR GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; IMP:UniProtKB.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; ISS:UniProtKB.
DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; ISS:UniProtKB.
DR GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
DR GO; GO:0009615; P:response to virus; IMP:MGI.
DR GO; GO:0010501; P:RNA secondary structure unwinding; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IDA:UniProtKB.
DR GO; GO:0090669; P:telomerase RNA stabilization; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
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; Antiviral defense; ATP-binding;
KW Cell projection; Chromosome; Coiled coil; Cytoplasm; Developmental protein;
KW Differentiation; DNA-binding; Helicase; Hydrolase; Immunity;
KW Innate immunity; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; RNA-binding; Telomere; Transcription; Transcription regulation;
KW Translation regulation; Transport.
FT CHAIN 1..1001
FT /note="ATP-dependent DNA/RNA helicase DHX36"
FT /id="PRO_0000247531"
FT DOMAIN 210..380
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 470..640
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..193
FT /note="Necessary for nuclear and nucleolar caps
FT localizations"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT REGION 1..97
FT /note="Required for the pre-miR-134 transport"
FT /evidence="ECO:0000250|UniProtKB:D4A2Z8"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..44
FT /note="Required for recruitment to cytoplasmic stress
FT granules"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT REGION 46..98
FT /note="Required for G4-DNA- and G4-RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT REGION 46..68
FT /note="DSM (DHX36-specific motif)"
FT /evidence="ECO:0000250|UniProtKB:Q05B79,
FT ECO:0000250|UniProtKB:Q9H2U1"
FT REGION 99..379
FT /note="RecA-like domain 1"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 258..310
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 380..621
FT /note="RecA-like domain 2"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 491..550
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 622..691
FT /note="WH domain"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 631..690
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 834..898
FT /note="OB-fold-like subdomains"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 842..853
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 863..893
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT COILED 120..147
FT /evidence="ECO:0000255"
FT MOTIF 327..330
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 510..521
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 226..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT BINDING 550
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT BINDING 595..598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT MOD_RES 940
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT MOD_RES 956
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT CONFLICT 29
FT /note="Missing (in Ref. 4; BAC98183)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="S -> T (in Ref. 4; BAC98183)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="E -> K (in Ref. 1; AAL47006)"
FT /evidence="ECO:0000305"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:6UP4"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 229..243
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 259..272
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 296..304
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 334..349
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 354..362
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 365..370
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 391..398
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:6UP3"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:6UP4"
FT HELIX 423..446
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 449..457
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 465..478
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 483..487
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 491..502
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 505..508
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 512..517
FT /evidence="ECO:0007829|PDB:6UP2"
FT TURN 526..528
FT /evidence="ECO:0007829|PDB:6UP3"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:6UP4"
FT STRAND 537..543
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 545..548
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 556..561
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 564..571
FT /evidence="ECO:0007829|PDB:6UP2"
FT TURN 572..575
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 576..583
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 586..594
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 597..608
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 610..614
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 623..626
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 630..638
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 644..649
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 657..669
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 681..687
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 693..704
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 708..719
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 731..742
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 748..764
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 767..777
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 781..800
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 805..807
FT /evidence="ECO:0007829|PDB:6UP4"
FT HELIX 812..814
FT /evidence="ECO:0007829|PDB:6UP2"
FT TURN 816..819
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 821..832
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 836..839
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 851..854
FT /evidence="ECO:0007829|PDB:6UP2"
FT TURN 855..857
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 858..862
FT /evidence="ECO:0007829|PDB:6UP2"
FT TURN 867..870
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 875..882
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 884..892
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 894..898
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 900..906
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 910..913
FT /evidence="ECO:0007829|PDB:6UP2"
FT TURN 915..917
FT /evidence="ECO:0007829|PDB:6UP3"
FT STRAND 920..923
FT /evidence="ECO:0007829|PDB:6UP2"
FT TURN 924..926
FT /evidence="ECO:0007829|PDB:6UP2"
FT STRAND 927..930
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 933..955
FT /evidence="ECO:0007829|PDB:6UP2"
FT HELIX 969..980
FT /evidence="ECO:0007829|PDB:6UP2"
SQ SEQUENCE 1001 AA; 113883 MW; 4DD9292011B8155A CRC64;
MSYDYHQSWS RDGGPRGSGQ GSSGGGGGGS RGSGGGGGGR GGRGRHPAHL KGREIGLWYA
KKQTQKNKEA ERQERAVVHM DERREEQIVQ LLNSVQAKTD KDSEAQISWF APEDHGYGTE
VSSEKKINSE KKLDNQEKKL LNQEKKTFRI TDKSYIDRDS EYLLQENEPN LSLDQHLLED
LQRKKTDPRY IEMQRFRKKL PSYGMQKELV NLINNHQVTV ISGETGCGKT TQVTQFILDN
YIERGKGSAC RIVCTQPRRI SAISVAERVA TERAESCGNG NSTGYQIRLQ SRLPRKQGSI
LYCTTGIILQ WLQSDSRLSS VSHIVLDEIH ERNLQSDVLM TVIKDLLHFR SDLKVILMSA
TLNAEKFSEY FGNCPMIHIP GFTFPVVEYL LEDIIEKIRY VPDQKEHRSQ FKRGFMQGHV
NRQEKEEKEA IYKERWPAYI KELRTRYSAS TVDVLQMMDD DKVDLNLIAA LIRYIVLEEE
DGAILVFLPG WDNISTLHDL LMSQVMFKSD KFLIIPLHSL MPTVNQTQVF KKTPPGVRKI
VIATNIAETS ITIDDVVYVI DGGKIKETHF DTQNNISTMS AEWVSKANAK QRKGRAGRVQ
PGHCYHLYNG LRASLLDDYQ LPEILRTPLE ELCLQIKILR LGGIAYFLSR LMDPPSNEAV
VLSIKHLMEL SALDKQEELT PLGVHLARLP VEPHIGKMIL FGALFCCLDP VLTIAASLSF
KDPFVIPLGK EKIADARRKE LAKETRSDHL TVVNAFEGWE EAKRRGFRYE KDYCWEYFLS
SNTLQMLHNM KGQFAEHLLG AGFVSSRSPK DPKANINSDN EKIIKAVICA GLYPKVAKIR
LNLGKKRKMV KVHTKSDGLV SIHPKSVNVE QTDFHYNWLI YHLKMRTSSI YLYDCTEVSP
YCLLFFGGDI SIQKDKDQEI IAVDEWIVFQ SPERIAHLVK GLRKELDSLL QEKIESPHPV
DWDDTKSRDC AVLSAILDLI KTQEKATPRN LPPRSQDGYY S
