ID DHX36_HUMAN Reviewed; 1008 AA. AC Q9H2U1; B2RB00; Q70JU3; Q8IYE5; Q9P240; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 2. DT 27-MAR-2024, entry version 195. DE RecName: Full=ATP-dependent DNA/RNA helicase DHX36 {ECO:0000305}; DE EC=3.6.4.12 {ECO:0000269|PubMed:16150737, ECO:0000269|PubMed:18842585, ECO:0000269|PubMed:21586581}; DE EC=3.6.4.13 {ECO:0000269|PubMed:18842585, ECO:0000269|PubMed:21846770, ECO:0000269|PubMed:25579584}; DE AltName: Full=DEAD/H box polypeptide 36 {ECO:0000303|PubMed:12198572}; DE AltName: Full=DEAH-box protein 36 {ECO:0000305}; DE AltName: Full=G4-resolvase-1 {ECO:0000303|PubMed:16150737}; DE Short=G4R1 {ECO:0000303|PubMed:16150737}; DE AltName: Full=MLE-like protein 1 {ECO:0000303|PubMed:14731398}; DE AltName: Full=RNA helicase associated with AU-rich element protein {ECO:0000303|PubMed:14731398}; GN Name=DHX36 {ECO:0000312|HGNC:HGNC:14410}; GN Synonyms=DDX36 {ECO:0000303|PubMed:12198572}, KIAA1488, MLEL1 GN {ECO:0000303|PubMed:14731398}, RHAU {ECO:0000303|PubMed:14731398}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT RP CYS-416. RC TISSUE=Brain; 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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AU-RICH RP RNA-BINDING, SUBCELLULAR LOCATION, ACTIVITY REGULATION, ALTERNATIVE RP SPLICING, TISSUE SPECIFICITY, INTERACTION WITH ELAVL1; ILF3; PARN; EXOSC3 RP AND EXOSC10, MUTAGENESIS OF GLU-335, VARIANT CYS-416, NUCLEAR LOCALIZATION RP SIGNAL, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=14731398; DOI=10.1016/s1097-2765(03)00481-7; RA Tran H., Schilling M., Wirbelauer C., Hess D., Nagamine Y.; RT "Facilitation of mRNA deadenylation and decay by the exosome-bound, DExH RT protein RHAU."; RL Mol. Cell 13:101-111(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS CYS-416 RP AND ASN-583. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-1008 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10819331; DOI=10.1093/dnares/7.2.143; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:143-150(2000). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, G-QUADRUPLEX DNA-BINDING, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16150737; DOI=10.1074/jbc.c500348200; RA Vaughn J.P., Creacy S.D., Routh E.D., Joyner-Butt C., Jenkins G.S., RA Pauli S., Nagamine Y., Akman S.A.; RT "The DEXH protein product of the DHX36 gene is the major source of RT tetramolecular quadruplex G4-DNA resolving activity in HeLa cell lysates."; RL J. Biol. Chem. 280:38117-38120(2005). RN [9] RP INTERACTION WITH AGO1 AND AGO2. RX PubMed=17932509; DOI=10.1038/sj.embor.7401088; RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., RA Urlaub H., Meister G.; RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein RT complexes in human cells."; RL EMBO Rep. 8:1052-1060(2007). RN [10] RP PROBABLE FUNCTION, INTERACTION WITH DDX5; DDX17; HDAC1 AND HDAC3, RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-335, AND REGION. RX PubMed=18279852; DOI=10.1016/j.yexcr.2008.01.006; RA Iwamoto F., Stadler M., Chalupnikova K., Oakeley E., Nagamine Y.; RT "Transcription-dependent nucleolar cap localization and possible nuclear RT function of DExH RNA helicase RHAU."; RL Exp. Cell Res. 314:1378-1391(2008). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, G-QUADRUPLEX DNA-BINDING, AND G-QUADRUPLEX RP RNA-BINDING. RX PubMed=18842585; DOI=10.1074/jbc.m806277200; RA Creacy S.D., Routh E.D., Iwamoto F., Nagamine Y., Akman S.A., Vaughn J.P.; RT "G4 resolvase 1 binds both DNA and RNA tetramolecular quadruplex with high RT affinity and is the major source of tetramolecular quadruplex G4-DNA and RT G4-RNA resolving activity in HeLa cell lysates."; RL J. Biol. Chem. 283:34626-34634(2008). RN [12] RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-335, AND RP REGION. RX PubMed=18854321; DOI=10.1074/jbc.m804857200; RA Chalupnikova K., Lattmann S., Selak N., Iwamoto F., Fujiki Y., Nagamine Y.; RT "Recruitment of the RNA helicase RHAU to stress granules via a unique RNA- RT binding domain."; RL J. Biol. Chem. 283:35186-35198(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-947, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [16] RP FUNCTION, TERC G-QUADRUPLEX RNA-BINDING, SUBCELLULAR LOCATION, REGION DSM RP MOTIF, AND MUTAGENESIS OF PRO-54; LEU-57; GLY-59; ILE-62 AND GLY-63. RX PubMed=20472641; DOI=10.1093/nar/gkq372; RA Lattmann S., Giri B., Vaughn J.P., Akman S.A., Nagamine Y.; RT "Role of the amino terminal RHAU-specific motif in the recognition and RT resolution of guanine quadruplex-RNA by the DEAH-box RNA helicase RHAU."; RL Nucleic Acids Res. 38:6219-6233(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP FUNCTION, TERC G-QUADRUPLEX RNA-BINDING, AND REGION. RX PubMed=21149580; DOI=10.1128/mcb.01033-10; RA Sexton A.N., Collins K.; RT "The 5' guanosine tracts of human telomerase RNA are recognized by the G- RT quadruplex binding domain of the RNA helicase DHX36 and function to RT increase RNA accumulation."; RL Mol. Cell. Biol. 31:736-743(2011). RN [19] RP FUNCTION, CATALYTIC ACTIVITY, AND G-QUADRUPLEX DNA-BINDING. RX PubMed=21586581; DOI=10.1093/nar/gkr234; RA Giri B., Smaldino P.J., Thys R.G., Creacy S.D., Routh E.D., Hantgan R.R., RA Lattmann S., Nagamine Y., Akman S.A., Vaughn J.P.; RT "G4 resolvase 1 tightly binds and unwinds unimolecular G4-DNA."; RL Nucleic Acids Res. 39:7161-7178(2011). RN [20] RP FUNCTION, TERC G-QUADRUPLEX RNA-BINDING, CATALYTIC ACTIVITY, COFACTOR, RP INTERACTION WITH TERT AND DKC1, REGION, AND MUTAGENESIS OF GLU-335. RX PubMed=21846770; DOI=10.1093/nar/gkr630; RA Lattmann S., Stadler M.B., Vaughn J.P., Akman S.A., Nagamine Y.; RT "The DEAH-box RNA helicase RHAU binds an intramolecular RNA G-quadruplex in RT TERC and associates with telomerase holoenzyme."; RL Nucleic Acids Res. 39:9390-9404(2011). RN [21] RP FUNCTION, AND G-QUADRUPLEX RNA-BINDING. RX PubMed=21993297; DOI=10.1093/nar/gkr849; RA Huang W., Smaldino P.J., Zhang Q., Miller L.D., Cao P., Stadelman K., RA Wan M., Giri B., Lei M., Nagamine Y., Vaughn J.P., Akman S.A., Sui G.; RT "Yin Yang 1 contains G-quadruplex structures in its promoter and 5'-UTR and RT its expression is modulated by G4 resolvase 1."; RL Nucleic Acids Res. 40:1033-1049(2012). RN [22] RP FUNCTION, TERC G-QUADRUPLEX RNA-BINDING, AND REGION DSM MOTIF. RX PubMed=22238380; DOI=10.1093/nar/gkr1306; RA Booy E.P., Meier M., Okun N., Novakowski S.K., Xiong S., Stetefeld J., RA McKenna S.A.; RT "The RNA helicase RHAU (DHX36) unwinds a G4-quadruplex in human telomerase RT RNA and promotes the formation of the P1 helix template boundary."; RL Nucleic Acids Res. 40:4110-4124(2012). RN [23] RP TERC G-QUADRUPLEX RNA-BINDING, G-QUADRUPLEX DNA-BINDING, AND REGION. RX PubMed=24151078; DOI=10.1074/jbc.m113.512970; RA Meier M., Patel T.R., Booy E.P., Marushchak O., Okun N., Deo S., Howard R., RA McEleney K., Harding S.E., Stetefeld J., McKenna S.A.; RT "Binding of G-quadruplexes to the N-terminal recognition domain of the RNA RT helicase associated with AU-rich element (RHAU)."; RL J. Biol. Chem. 288:35014-35027(2013). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161 AND SER-963, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [25] RP FUNCTION, G-QUADRUPLEX RNA-BINDING, RNA-BINDING, AND REGION DSM MOTIF. RX PubMed=24369427; DOI=10.1093/nar/gkt1340; RA Booy E.P., Howard R., Marushchak O., Ariyo E.O., Meier M., Novakowski S.K., RA Deo S.R., Dzananovic E., Stetefeld J., McKenna S.A.; RT "The RNA helicase RHAU (DHX36) suppresses expression of the transcription RT factor PITX1."; RL Nucleic Acids Res. 42:3346-3361(2014). RN [26] RP FUNCTION, G-QUADRUPLEX RNA-BINDING, AU-RICH RNA-BINDING, AND INTERACTION RP WITH ELAVL1. 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). RN [27] RP FUNCTION, CATALYTIC ACTIVITY, AND G-QUADRUPLEX RNA-BINDING. RX PubMed=25579584; DOI=10.1007/978-1-4939-2214-7_9; RA Booy E.P., McRae E.K., McKenna S.A.; RT "Biochemical characterization of G4 quadruplex telomerase RNA unwinding by RT the RNA helicase RHAU."; RL Methods Mol. Biol. 1259:125-135(2015). RN [28] RP INTERACTION WITH ERCC6. RX PubMed=26030138; DOI=10.1371/journal.pone.0128558; RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G., RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.; RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin RT Dynamics."; RL PLoS ONE 10:E0128558-E0128558(2015). RN [29] RP G-QUADRUPLEX RNA-BINDING, G-QUADRUPLEX DNA-BINDING, AND REGION DSM MOTIF. RX PubMed=26649896; DOI=10.1371/journal.pone.0144510; RA Ariyo E.O., Booy E.P., Patel T.R., Dzananovic E., McRae E.K., Meier M., RA McEleney K., Stetefeld J., McKenna S.A.; RT "Biophysical Characterization of G-Quadruplex Recognition in the PITX1 mRNA RT by the Specificity Domain of the Helicase RHAU."; RL PLoS ONE 10:E0144510-E0144510(2015). RN [30] RP FUNCTION, AND G-QUADRUPLEX RNA-BINDING. RX PubMed=27940037; DOI=10.1016/j.jmb.2016.11.033; RA Newman M., Sfaxi R., Saha A., Monchaud D., Teulade-Fichou M.P., Vagner S.; RT "The G-Quadruplex-Specific RNA Helicase DHX36 Regulates p53 Pre-mRNA 3'-End RT Processing Following UV-Induced DNA Damage."; RL J. Mol. Biol. 429:3121-3131(2017). RN [31] {ECO:0007744|PDB:2N16, ECO:0007744|PDB:2N21} RP STRUCTURE BY NMR OF 53-70 IN COMPLEX WITH G-QUADRUPLEX DNA, FUNCTION, RP G-QUADRUPLEX DNA-BINDING, G-QUADRUPLEX RNA-BINDING, REGION DSM MOTIF, AND RP MUTAGENESIS OF GLY-55; GLY-59; GLY-63; TRP-65 AND TYR-66. RX PubMed=26195789; DOI=10.1073/pnas.1422605112; RA Heddi B., Cheong V.V., Martadinata H., Phan A.T.; RT "Insights into G-quadruplex specific recognition by the DEAH-box helicase RT RHAU: Solution structure of a peptide-quadruplex complex."; RL Proc. Natl. Acad. Sci. U.S.A. 112:9608-9613(2015). CC -!- FUNCTION: Multifunctional ATP-dependent helicase that unwinds G- CC quadruplex (G4) structures (PubMed:16150737, PubMed:18854321, CC PubMed:20472641, PubMed:21586581). Plays a role in many biological CC processes such as genomic integrity, gene expression regulations and as CC a sensor to initiate antiviral responses (PubMed:14731398, CC PubMed:18279852, PubMed:21993297, PubMed:22238380, PubMed:25579584). G4 CC structures correspond to helical structures containing guanine tetrads CC (By similarity). Binds with high affinity to and unwinds G4 structures CC that are formed in nucleic acids (G4-ADN and G4-RNA) (PubMed:16150737, CC PubMed:18842585, PubMed:20472641, PubMed:21586581, PubMed:24369427, CC PubMed:26195789). Plays a role in genomic integrity (PubMed:22238380). CC Converts the G4-RNA structure present in telomerase RNA template CC component (TREC) into a double-stranded RNA to promote P1 helix CC formation that acts as a template boundary ensuring accurate reverse CC transcription (PubMed:20472641, PubMed:21149580, PubMed:21846770, CC PubMed:22238380, PubMed:24151078, PubMed:25579584). Plays a role in CC transcriptional regulation (PubMed:21586581, PubMed:21993297). Resolves CC G4-DNA structures in promoters of genes, such as YY1, KIT/c-kit and CC ALPL and positively regulates their expression (PubMed:21993297). Plays CC a role in post-transcriptional regulation (PubMed:27940037). Unwinds a CC G4-RNA structure located in the 3'-UTR polyadenylation site of the pre- CC mRNA TP53 and stimulates TP53 pre-mRNA 3'-end processing in response to CC ultraviolet (UV)-induced DNA damage (PubMed:27940037). Binds to the CC precursor-microRNA-134 (pre-miR-134) terminal loop and regulates its CC transport into the synapto-dendritic compartment (By similarity). CC Involved in the pre-miR-134-dependent inhibition of target gene CC expression and the control of dendritic spine size (By similarity). CC Plays a role in the regulation of cytoplasmic mRNA translation and mRNA CC stability (PubMed:24369427, PubMed:26489465). Binds to both G4-RNA CC structures and alternative non-quadruplex-forming sequence within the CC 3'-UTR of the PITX1 mRNA regulating negatively PITX1 protein expression CC (PubMed:24369427). Binds to both G4-RNA structure in the 5'-UTR and AU- CC rich elements (AREs) localized in the 3'-UTR of NKX2-5 mRNA to either CC stimulate protein translation or induce mRNA decay in an ELAVL1- CC dependent manner, respectively (PubMed:26489465). Binds also to ARE CC sequences present in several mRNAs mediating exosome-mediated 3'-5' CC mRNA degradation (PubMed:14731398, PubMed:18279852). Involved in CC cytoplasmic urokinase-type plasminogen activator (uPA) mRNA decay CC (PubMed:14731398). Component of a multi-helicase-TICAM1 complex that CC acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and CC plays a role in the activation of a cascade of antiviral responses CC including the induction of pro-inflammatory cytokines via the adapter CC molecule TICAM1 (By similarity). Required for early embryonic CC development and hematopoiesis. Involved in the regulation of CC cardioblast differentiation and proliferation during heart development. CC Involved in spermatogonia differentiation. May play a role in CC ossification (By similarity). {ECO:0000250|UniProtKB:D4A2Z8, CC ECO:0000250|UniProtKB:Q05B79, ECO:0000250|UniProtKB:Q8VHK9, CC ECO:0000269|PubMed:14731398, ECO:0000269|PubMed:16150737, CC ECO:0000269|PubMed:18279852, ECO:0000269|PubMed:18842585, CC ECO:0000269|PubMed:18854321, ECO:0000269|PubMed:20472641, CC ECO:0000269|PubMed:21149580, ECO:0000269|PubMed:21586581, CC ECO:0000269|PubMed:21846770, ECO:0000269|PubMed:21993297, CC ECO:0000269|PubMed:22238380, ECO:0000269|PubMed:24151078, CC ECO:0000269|PubMed:24369427, ECO:0000269|PubMed:25579584, CC ECO:0000269|PubMed:26195789, ECO:0000269|PubMed:26489465, CC ECO:0000269|PubMed:27940037}. 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=3.6.4.12; CC Evidence={ECO:0000269|PubMed:16150737, ECO:0000269|PubMed:18842585, CC ECO:0000269|PubMed:21586581, ECO:0000269|PubMed:21846770, CC ECO:0000269|PubMed:25579584}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CC Evidence={ECO:0000269|PubMed:16150737, ECO:0000269|PubMed:18842585, CC ECO:0000269|PubMed:21586581, ECO:0000269|PubMed:21846770, CC ECO:0000269|PubMed:25579584}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:16150737, ECO:0000269|PubMed:21846770}; 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:0000269|PubMed:14731398}. 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 (By similarity). CC Interacts (via C-terminus) with TICAM1 (via TIR domain) (By CC similarity). Interacts (via C-terminus) with DDX21; this interaction CC serves as bridges to TICAM1 (By similarity). Interacts with TERT; this CC interaction is dependent on the ability of DHX36 to bind to the G- CC quadruplex RNA (G4-RNA) structure present in the telomerase RNA CC template component (TERC) (PubMed:21846770). Interacts with DKC1; this CC interaction is dependent on the ability of DHX36 to bind to the G4-RNA CC structure present in TERC (PubMed:21846770). Interacts with PARN; this CC interaction stimulates PARN to enhance uPA mRNA decay CC (PubMed:14731398). Interacts with EXOSC3; this interaction occurs in a CC RNase-insensitive manner (PubMed:14731398). Interacts with EXOSC10; CC this interaction occurs in a RNase-insensitive manner CC (PubMed:14731398). Interacts with ILF3; this interaction occurs in a CC RNA-dependent manner (PubMed:14731398). Interacts with ELAVL1; this CC interaction occurs in an RNA-dependent manner (PubMed:14731398, CC PubMed:26489465). Interacts with DDX5; this interaction occurs in a CC RNA-dependent manner (PubMed:18279852). Interacts with DDX17; this CC interaction occurs in a RNA-dependent manner (PubMed:18279852). CC Interacts with HDAC1; this interaction occurs in a RNA-dependent manner CC (PubMed:18279852). Interacts with HDAC3; this interaction occurs in a CC RNA-dependent manner (PubMed:18279852). Interacts with HDAC4 (By CC similarity). Interacts with AGO1 (PubMed:17932509). Interacts with AGO2 CC (PubMed:17932509). Interacts with ERCC6 (PubMed:26030138). CC {ECO:0000250|UniProtKB:Q8VHK9, ECO:0000269|PubMed:14731398, CC ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:18279852, CC ECO:0000269|PubMed:21846770, ECO:0000269|PubMed:26030138, CC ECO:0000269|PubMed:26489465}. CC -!- INTERACTION: CC Q9H2U1-3; P30519: HMOX2; NbExp=3; IntAct=EBI-25868628, EBI-712096; CC Q9H2U1-3; P62826: RAN; NbExp=3; IntAct=EBI-25868628, EBI-286642; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18279852, CC ECO:0000269|PubMed:18854321}. Cytoplasm {ECO:0000269|PubMed:18279852, CC ECO:0000269|PubMed:18854321}. Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q8VHK9}. Cytoplasm, Stress granule CC {ECO:0000269|PubMed:18854321}. Nucleus speckle CC {ECO:0000269|PubMed:18279852}. Chromosome, telomere CC {ECO:0000269|PubMed:20472641}. Mitochondrion CC {ECO:0000250|UniProtKB:Q8VHK9}. 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 (PubMed:18279852). Colocalizes with SRSF2 in nuclear speckles CC (PubMed:18279852). Colocalizes with DDX5 in nucleolar caps upon CC transcription inhibition (PubMed:18279852). Accumulates and colocalized CC with TIA1 in cytoplasmic stress granules (SGs) in an arsenite-, heat CC shock- and RNA-binding-dependent manner (PubMed:18854321). Shuttles CC into and out of SGs in an ATPase-dependent manner (PubMed:18854321). CC Colocalizes in the cytosol with the multi-helicase-TICAM1 complex that CC translocates to the mitochondria upon poly(I:C) RNA ligand stimulation CC (By similarity). {ECO:0000250|UniProtKB:Q8VHK9, CC ECO:0000269|PubMed:18279852, ECO:0000269|PubMed:18854321}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus CC {ECO:0000269|PubMed:14731398}. Cytoplasm {ECO:0000269|PubMed:14731398}. CC Note=Preferentially localized in the nucleus (PubMed:14731398). CC Excluded from nucleoli (PubMed:14731398). CC {ECO:0000269|PubMed:14731398}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus CC {ECO:0000269|PubMed:14731398}. Cytoplasm {ECO:0000269|PubMed:14731398}. CC Note=Preferentially localized in the cytoplasm (PubMed:14731398). CC Excluded from nucleoli (PubMed:14731398). CC {ECO:0000269|PubMed:14731398}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=Nuclear isoform {ECO:0000303|PubMed:14731398}; CC IsoId=Q9H2U1-1; Sequence=Displayed; CC Name=2; Synonyms=Cytoplasmic isoform, RHAU-delta 14 CC {ECO:0000303|PubMed:14731398}; CC IsoId=Q9H2U1-2; Sequence=VSP_020006; CC Name=3; CC IsoId=Q9H2U1-3; Sequence=VSP_020007; CC -!- TISSUE SPECIFICITY: Highly expressed in testis. CC {ECO:0000269|PubMed:12198572, ECO:0000269|PubMed:14731398}. 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, selectively CC bind to Myc-promoter G4-DNA-containing structure in an ATP-dependent CC manner. Upon G4-DNA-binding, DHX36 pulls on DSM in the 3'-direction, CC inducing rearrangement of the RecA-like 1 and 2 and the degenerate- CC winged-helix (WH) regions; these rearrangements are propbably CC responsible for the ATP-independent repetitive G4-DNA unfolding CC activity, one residue at a time. Upon resolving of G4-DNA into separate CC nucleotide strands, and ATP hydrolysis, the apoprotein of DHX36 seems CC incompatible with G4-DNA-binding (By similarity). The N-terminus is CC necessary for its recruitment to cytoplasmic stress granules (SGs) upon CC arsenite-induced treatment (PubMed:18854321). CC {ECO:0000250|UniProtKB:Q05B79, ECO:0000269|PubMed:18854321}. CC -!- MISCELLANEOUS: [Isoform 2]: More unstable than isoform 1. CC {ECO:0000269|PubMed:14731398}. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF217190; AAG36783.1; -; mRNA. DR EMBL; AJ577133; CAE11802.1; -; mRNA. DR EMBL; AJ577134; CAE11803.1; -; mRNA. DR EMBL; AK314435; BAG37047.1; -; mRNA. DR EMBL; AC018452; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC134026; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW78761.1; -; Genomic_DNA. DR EMBL; BC036035; AAH36035.1; -; mRNA. DR EMBL; AB040921; BAA96012.1; -; mRNA. DR CCDS; CCDS3171.1; -. [Q9H2U1-1] DR CCDS; CCDS54657.1; -. [Q9H2U1-2] DR PIR; D56236; D56236. DR RefSeq; NP_001107869.1; NM_001114397.1. [Q9H2U1-2] DR RefSeq; NP_065916.2; NM_020865.2. [Q9H2U1-1] DR PDB; 2N16; NMR; -; A=53-70. DR PDB; 2N21; NMR; -; A=53-70. DR PDB; 6Q6R; X-ray; 1.50 A; E/F/G/H=53-81. DR PDBsum; 2N16; -. DR PDBsum; 2N21; -. DR PDBsum; 6Q6R; -. DR AlphaFoldDB; Q9H2U1; -. DR SMR; Q9H2U1; -. DR BioGRID; 128022; 310. DR IntAct; Q9H2U1; 51. DR MINT; Q9H2U1; -. DR STRING; 9606.ENSP00000417078; -. DR ChEMBL; CHEMBL2040704; -. DR GlyGen; Q9H2U1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H2U1; -. DR MetOSite; Q9H2U1; -. DR PhosphoSitePlus; Q9H2U1; -. DR SwissPalm; Q9H2U1; -. DR BioMuta; DHX36; -. DR DMDM; 313104099; -. DR EPD; Q9H2U1; -. DR jPOST; Q9H2U1; -. DR MassIVE; Q9H2U1; -. DR MaxQB; Q9H2U1; -. DR PaxDb; 9606-ENSP00000417078; -. DR PeptideAtlas; Q9H2U1; -. DR ProteomicsDB; 80591; -. [Q9H2U1-1] DR ProteomicsDB; 80592; -. [Q9H2U1-2] DR ProteomicsDB; 80593; -. [Q9H2U1-3] DR Pumba; Q9H2U1; -. DR Antibodypedia; 33625; 208 antibodies from 27 providers. DR DNASU; 170506; -. DR Ensembl; ENST00000308361.10; ENSP00000309296.6; ENSG00000174953.14. [Q9H2U1-3] DR Ensembl; ENST00000329463.9; ENSP00000330113.5; ENSG00000174953.14. [Q9H2U1-2] DR Ensembl; ENST00000496811.6; ENSP00000417078.1; ENSG00000174953.14. [Q9H2U1-1] DR GeneID; 170506; -. DR KEGG; hsa:170506; -. DR MANE-Select; ENST00000496811.6; ENSP00000417078.1; NM_020865.3; NP_065916.2. DR UCSC; uc003ezy.5; human. [Q9H2U1-1] DR AGR; HGNC:14410; -. DR CTD; 170506; -. DR DisGeNET; 170506; -. DR GeneCards; DHX36; -. DR HGNC; HGNC:14410; DHX36. DR HPA; ENSG00000174953; Low tissue specificity. DR MIM; 612767; gene. DR neXtProt; NX_Q9H2U1; -. DR OpenTargets; ENSG00000174953; -. DR PharmGKB; PA27223; -. DR VEuPathDB; HostDB:ENSG00000174953; -. DR eggNOG; KOG0920; Eukaryota. DR GeneTree; ENSGT00940000156903; -. DR InParanoid; Q9H2U1; -. DR OMA; WLQSDKH; -. DR OrthoDB; 1095660at2759; -. DR PhylomeDB; Q9H2U1; -. DR TreeFam; TF324744; -. DR PathwayCommons; Q9H2U1; -. DR Reactome; R-HSA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production. DR SignaLink; Q9H2U1; -. DR SIGNOR; Q9H2U1; -. DR BioGRID-ORCS; 170506; 643 hits in 1191 CRISPR screens. DR ChiTaRS; DHX36; human. DR GeneWiki; DHX36; -. DR GenomeRNAi; 170506; -. DR Pharos; Q9H2U1; Tbio. DR PRO; PR:Q9H2U1; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9H2U1; Protein. DR Bgee; ENSG00000174953; Expressed in sperm and 194 other cell types or tissues. DR ExpressionAtlas; Q9H2U1; baseline and differential. DR GO; GO:0030424; C:axon; ISS:UniProtKB. DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0030425; C:dendrite; ISS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA: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; IDA:UniProtKB. DR GO; GO:0003678; F:DNA helicase activity; IDA: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; IDA:UniProtKB. DR GO; GO:0042826; F:histone deacetylase binding; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB. DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:UniProtKB. DR GO; GO:0070883; F:pre-miRNA binding; ISS:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0003724; F:RNA helicase activity; IDA: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; IDA:UniProtKB. DR GO; GO:0070034; F:telomerase RNA binding; IDA:UniProtKB. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB. DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IMP:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:1903843; P:cellular response to arsenite ion; IDA:UniProtKB. DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB. DR GO; GO:0034644; P:cellular response to UV; IMP: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; IDA:UniProtKB. DR GO; GO:0001503; P:ossification; ISS:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB. DR GO; GO:0051891; P:positive regulation of cardioblast differentiation; ISS:UniProtKB. DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IMP:UniProtKB. DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB. DR GO; GO:1901534; P:positive regulation of hematopoietic progenitor cell differentiation; ISS:UniProtKB. DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IMP:UniProtKB. 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; IMP:UniProtKB. DR GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; IEA:Ensembl. DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:UniProtKB. DR GO; GO:0032206; P:positive regulation of telomere maintenance; IMP:UniProtKB. DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB. DR GO; GO:0043488; P:regulation of mRNA stability; IMP:UniProtKB. DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IMP:UniProtKB. DR GO; GO:0043330; P:response to exogenous dsRNA; IEA:Ensembl. DR GO; GO:0010501; P:RNA secondary structure unwinding; IDA:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR GO; GO:0090669; P:telomerase RNA stabilization; IDA:BHF-UCL. DR CDD; cd17981; DEXHc_DHX36; 1. DR CDD; cd18791; SF2_C_RHA; 1. DR Gene3D; 1.20.120.1080; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR048333; HA2_WH. DR InterPro; IPR007502; Helicase-assoc_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR18934:SF237; ATP-DEPENDENT DNA_RNA HELICASE DHX36; 1. DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF21010; HA2_C; 1. DR Pfam; PF04408; HA2_N; 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; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR Genevisible; Q9H2U1; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; KW Antiviral defense; ATP-binding; Cell projection; Chromosome; Coiled coil; KW Cytoplasm; Developmental protein; Differentiation; DNA-binding; Helicase; KW Hydrolase; Immunity; Innate immunity; Magnesium; Metal-binding; KW Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Repressor; RNA-binding; Telomere; KW Transcription; Transcription regulation; Translation regulation; Transport. FT CHAIN 1..1008 FT /note="ATP-dependent DNA/RNA helicase DHX36" FT /id="PRO_0000247530" FT DOMAIN 217..387 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 477..647 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 1..200 FT /note="Necessary for nuclear and nucleolar caps FT localizations" FT /evidence="ECO:0000269|PubMed:18279852" FT REGION 1..104 FT /note="Required for the pre-miR-134 transport" FT /evidence="ECO:0000250|UniProtKB:D4A2Z8" FT REGION 1..58 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1..51 FT /note="Required for recruitment to cytoplasmic stress FT granules" FT /evidence="ECO:0000269|PubMed:18854321" FT REGION 53..105 FT /note="Required for G4-DNA- and G4-RNA-binding" FT /evidence="ECO:0000269|PubMed:21149580, FT ECO:0000269|PubMed:21846770, ECO:0000269|PubMed:24151078" FT REGION 53..75 FT /note="DSM (DHX36-specific motif)" FT /evidence="ECO:0000269|PubMed:20472641, FT ECO:0000269|PubMed:22238380, ECO:0000269|PubMed:24369427, FT ECO:0000269|PubMed:26195789, ECO:0000269|PubMed:26649896" FT REGION 106..386 FT /note="RecA-like domain 1" FT /evidence="ECO:0000250|UniProtKB:Q05B79" FT REGION 265..317 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 387..628 FT /note="RecA-like domain 2" FT /evidence="ECO:0000250|UniProtKB:Q05B79" FT REGION 498..557 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 629..698 FT /note="WH domain" FT /evidence="ECO:0000250|UniProtKB:Q05B79" FT REGION 638..697 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 841..905 FT /note="OB-fold-like subdomains" FT /evidence="ECO:0000250|UniProtKB:Q05B79" FT REGION 849..860 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 870..900 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 72..157 FT /evidence="ECO:0000255" FT MOTIF 334..337 FT /note="DEAH box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT MOTIF 517..528 FT /note="Nuclear localization signal" FT /evidence="ECO:0000303|PubMed:14731398" FT BINDING 233..238 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q05B79" FT BINDING 335 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q05B79" FT BINDING 337 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q05B79" FT BINDING 557 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q05B79" FT BINDING 602..605 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q05B79" FT MOD_RES 161 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 947 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 963 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 517..530 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14731398" FT /id="VSP_020006" FT VAR_SEQ 737..765 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020007" FT VARIANT 151 FT /note="E -> K (in dbSNP:rs1058299)" FT /id="VAR_027140" FT VARIANT 416 FT /note="S -> C (in dbSNP:rs9438)" FT /evidence="ECO:0000269|PubMed:12198572, FT ECO:0000269|PubMed:14731398, ECO:0000269|PubMed:15489334" FT /id="VAR_027141" FT VARIANT 583 FT /note="I -> N (in dbSNP:rs17853513)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_027142" FT MUTAGEN 54 FT /note="P->G: Reduces G4-RNA binding; when associated with FT A-57, A-59, A-62 and A-63." FT /evidence="ECO:0000269|PubMed:20472641" FT MUTAGEN 55 FT /note="G->L: Inhibits G4-DNA-binding; when associated with FT L-59 and L-63." FT /evidence="ECO:0000269|PubMed:26195789" FT MUTAGEN 57 FT /note="L->A: Reduces G4-RNA-binding; when associated with FT G-54, A-59, A-62 and A-63." FT /evidence="ECO:0000269|PubMed:20472641" FT MUTAGEN 59 FT /note="G->A: Reduces G4-RNA-binding; when associated with FT G-54, A-57, A-62 and A-63." FT /evidence="ECO:0000269|PubMed:20472641" FT MUTAGEN 59 FT /note="G->L: Inhibits G4-DNA-binding; when associated with FT L-55 and L-63." FT /evidence="ECO:0000269|PubMed:26195789" FT MUTAGEN 59 FT /note="G->P: Greatly reduces G4-RNA-binding; when FT associated with P-63." FT /evidence="ECO:0000269|PubMed:20472641" FT MUTAGEN 62 FT /note="I->A: Reduces G4-RNA-binding; when associated with FT G-54, A-57, A-59 and A-63." FT /evidence="ECO:0000269|PubMed:20472641" FT MUTAGEN 63 FT /note="G->A: Reduces G4-RNA-binding; when associated with FT G-54, A-57, A-59 and A-62." FT /evidence="ECO:0000269|PubMed:20472641" FT MUTAGEN 63 FT /note="G->L: Inhibits G4-DNA-binding; when associated with FT L-55 and L-59." FT /evidence="ECO:0000269|PubMed:26195789" FT MUTAGEN 63 FT /note="G->P: Greatly reduces G4-RNA-binding; when FT associated with P-59." FT /evidence="ECO:0000269|PubMed:20472641" FT MUTAGEN 65 FT /note="W->A: Does not inhibit G4-DNA-binding; when FT associated with A-66." FT /evidence="ECO:0000269|PubMed:26195789" FT MUTAGEN 66 FT /note="Y->A: Does not inhibit G4-DNA-binding; when FT associated with A-65." FT /evidence="ECO:0000269|PubMed:26195789" FT MUTAGEN 335 FT /note="E->A: Loss of ATPase activity; results in an FT increased in G4-DNA- and G4-RNA-binding stabilities, FT increases localization in cytoplasmic stress granules and FT loss of mRNA deadenylation and mRNA decay." FT /evidence="ECO:0000269|PubMed:14731398, FT ECO:0000269|PubMed:18279852, ECO:0000269|PubMed:18854321, FT ECO:0000269|PubMed:21846770" FT HELIX 60..67 FT /evidence="ECO:0007829|PDB:6Q6R" SQ SEQUENCE 1008 AA; 114760 MW; 66A28A1FE93C62AE CRC64; MSYDYHQNWG RDGGPRSSGG GYGGGPAGGH GGNRGSGGGG GGGGGGRGGR GRHPGHLKGR EIGMWYAKKQ GQKNKEAERQ ERAVVHMDER REEQIVQLLN SVQAKNDKES EAQISWFAPE DHGYGTEVST KNTPCSENKL DIQEKKLINQ EKKMFRIRNR SYIDRDSEYL LQENEPDGTL DQKLLEDLQK KKNDLRYIEM QHFREKLPSY GMQKELVNLI DNHQVTVISG ETGCGKTTQV TQFILDNYIE RGKGSACRIV CTQPRRISAI SVAERVAAER AESCGSGNST GYQIRLQSRL PRKQGSILYC TTGIILQWLQ SDPYLSSVSH IVLDEIHERN LQSDVLMTVV KDLLNFRSDL KVILMSATLN AEKFSEYFGN CPMIHIPGFT FPVVEYLLED VIEKIRYVPE QKEHRSQFKR GFMQGHVNRQ EKEEKEAIYK ERWPDYVREL RRRYSASTVD VIEMMEDDKV DLNLIVALIR YIVLEEEDGA ILVFLPGWDN ISTLHDLLMS QVMFKSDKFL IIPLHSLMPT VNQTQVFKRT PPGVRKIVIA TNIAETSITI DDVVYVIDGG KIKETHFDTQ NNISTMSAEW VSKANAKQRK GRAGRVQPGH CYHLYNGLRA SLLDDYQLPE ILRTPLEELC LQIKILRLGG IAYFLSRLMD PPSNEAVLLS IRHLMELNAL DKQEELTPLG VHLARLPVEP HIGKMILFGA LFCCLDPVLT IAASLSFKDP FVIPLGKEKI ADARRKELAK DTRSDHLTVV NAFEGWEEAR RRGFRYEKDY CWEYFLSSNT LQMLHNMKGQ FAEHLLGAGF VSSRNPKDPE SNINSDNEKI IKAVICAGLY PKVAKIRLNL GKKRKMVKVY TKTDGLVAVH PKSVNVEQTD FHYNWLIYHL KMRTSSIYLY DCTEVSPYCL LFFGGDISIQ KDNDQETIAV DEWIVFQSPA RIAHLVKELR KELDILLQEK IESPHPVDWN DTKSRDCAVL SAIIDLIKTQ EKATPRNFPP RFQDGYYS //