DHX36_HUMAN
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 03-AUG-2022, entry version 186.
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,
GN MLEL1 {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}.
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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; 268.
DR IntAct; Q9H2U1; 44.
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 BioMuta; DHX36; -.
DR DMDM; 313104099; -.
DR EPD; Q9H2U1; -.
DR jPOST; Q9H2U1; -.
DR MassIVE; Q9H2U1; -.
DR MaxQB; Q9H2U1; -.
DR PaxDb; Q9H2U1; -.
DR PeptideAtlas; Q9H2U1; -.
DR PRIDE; Q9H2U1; -.
DR ProteomicsDB; 80591; -. [Q9H2U1-1]
DR ProteomicsDB; 80592; -. [Q9H2U1-2]
DR ProteomicsDB; 80593; -. [Q9H2U1-3]
DR Antibodypedia; 33625; 182 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 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; GKMILMS; -.
DR OrthoDB; 278674at2759; -.
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; 624 hits in 1097 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 192 other tissues.
DR ExpressionAtlas; Q9H2U1; baseline and differential.
DR Genevisible; Q9H2U1; HS.
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: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:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; 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 from RNA polymerase II promoter; 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 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; 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
