DHX30_HUMAN
ID DHX30_HUMAN Reviewed; 1194 AA.
AC Q7L2E3; A8K5F1; O94965; Q7Z753; Q96CH4; Q9NUQ0;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=ATP-dependent RNA helicase DHX30 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000269|PubMed:29100085};
DE AltName: Full=DEAH box protein 30;
GN Name=DHX30; Synonyms=DDX30, KIAA0890;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Placenta, and Teratocarcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Lymph, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=16825194; DOI=10.1074/jbc.m604501200;
RA Wang Y., Bogenhagen D.F.;
RT "Human mitochondrial DNA nucleoids are linked to protein folding machinery
RT and metabolic enzymes at the mitochondrial inner membrane.";
RL J. Biol. Chem. 281:25791-25802(2006).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION, ASSOCIATION WITH MITOCHONDRIAL DNA, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18063578; DOI=10.1074/jbc.m708444200;
RA Bogenhagen D.F., Rousseau D., Burke S.;
RT "The layered structure of human mitochondrial DNA nucleoids.";
RL J. Biol. Chem. 283:3665-3675(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-380, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH GRSF1; DDX28; FASTKD2 AND
RP FASTKD5, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25683715; DOI=10.1016/j.celrep.2015.01.030;
RA Antonicka H., Shoubridge E.A.;
RT "Mitochondrial RNA granules are centers for post-transcriptional RNA
RT processing and ribosome biogenesis.";
RL Cell Rep. 10:920-932(2015).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP STRUCTURE BY NMR OF 42-148.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the double-stranded RNA binding domain in KIAA0890
RT protein.";
RL Submitted (JUN-2006) to the PDB data bank.
RN [17]
RP INVOLVEMENT IN NEDMIAL, VARIANTS NEDMIAL HIS-493; ARG-562; ASP-781;
RP TRP-782; CYS-785 AND HIS-785, CHARACTERIZATION OF VARIANTS NEDMIAL HIS-493;
RP ARG-562; ASP-781; TRP-782; CYS-785 AND HIS-785, FUNCTION, CATALYTIC
RP ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=29100085; DOI=10.1016/j.ajhg.2017.09.014;
RG DDD study;
RG C4RCD Research Group;
RA Lessel D., Schob C., Kuery S., Reijnders M.R.F., Harel T., Eldomery M.K.,
RA Coban-Akdemir Z., Denecke J., Edvardson S., Colin E., Stegmann A.P.A.,
RA Gerkes E.H., Tessarech M., Bonneau D., Barth M., Besnard T., Cogne B.,
RA Revah-Politi A., Strom T.M., Rosenfeld J.A., Yang Y., Posey J.E.,
RA Immken L., Oundjian N., Helbig K.L., Meeks N., Zegar K., Morton J.,
RA Schieving J.H., Claasen A., Huentelman M., Narayanan V., Ramsey K.,
RA Brunner H.G., Elpeleg O., Mercier S., Bezieau S., Kubisch C., Kleefstra T.,
RA Kindler S., Lupski J.R., Kreienkamp H.J.;
RT "De Novo Missense Mutations in DHX30 Impair Global Translation and Cause a
RT Neurodevelopmental Disorder.";
RL Am. J. Hum. Genet. 101:716-724(2017).
RN [18]
RP VARIANTS NEDMIAL HIS-493; ARG-562 AND TRP-782.
RX PubMed=28327206; DOI=10.1186/s13073-017-0412-6;
RA Eldomery M.K., Coban-Akdemir Z., Harel T., Rosenfeld J.A., Gambin T.,
RA Stray-Pedersen A., Kuery S., Mercier S., Lessel D., Denecke J.,
RA Wiszniewski W., Penney S., Liu P., Bi W., Lalani S.R., Schaaf C.P.,
RA Wangler M.F., Bacino C.A., Lewis R.A., Potocki L., Graham B.H.,
RA Belmont J.W., Scaglia F., Orange J.S., Jhangiani S.N., Chiang T.,
RA Doddapaneni H., Hu J., Muzny D.M., Xia F., Beaudet A.L., Boerwinkle E.,
RA Eng C.M., Plon S.E., Sutton V.R., Gibbs R.A., Posey J.E., Yang Y.,
RA Lupski J.R.;
RT "Lessons learned from additional research analyses of unsolved clinical
RT exome cases.";
RL Genome Med. 9:26-26(2017).
CC -!- FUNCTION: RNA-dependent helicase (PubMed:29100085). Plays an important
CC role in the assembly of the mitochondrial large ribosomal subunit
CC (PubMed:25683715, PubMed:29100085). Required for optimal function of
CC the zinc-finger antiviral protein ZC3HAV1 (By similarity). Associates
CC with mitochondrial DNA (PubMed:18063578). Involved in nervous system
CC development and differentiation through its involvement in the up-
CC regulation of a number of genes which are required for neurogenesis,
CC including GSC, NCAM1, neurogenin, and NEUROD (By similarity).
CC {ECO:0000250|UniProtKB:Q5BJS0, ECO:0000250|UniProtKB:Q99PU8,
CC ECO:0000269|PubMed:18063578, ECO:0000269|PubMed:25683715,
CC ECO:0000269|PubMed:29100085}.
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:29100085};
CC -!- SUBUNIT: Identified in a complex with TFAM and SSBP1. Interacts with
CC AGO1 and AGO2. Interacts (via N-terminus) with ZC3HAV1 (via N-terminal
CC domain) in an RNA-independent manner (By similarity). Found in a
CC complex with GRSF1, DDX28, FASTKD2 and FASTKD5 (PubMed:25683715).
CC {ECO:0000250|UniProtKB:Q5BJS0, ECO:0000269|PubMed:16825194,
CC ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:25683715}.
CC -!- INTERACTION:
CC Q7L2E3; Q96C10: DHX58; NbExp=2; IntAct=EBI-1211456, EBI-744193;
CC Q7L2E3; P19525: EIF2AK2; NbExp=4; IntAct=EBI-1211456, EBI-640775;
CC Q7L2E3; Q9Y6K5: OAS3; NbExp=2; IntAct=EBI-1211456, EBI-6115729;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29100085}.
CC Mitochondrion {ECO:0000269|PubMed:16825194,
CC ECO:0000269|PubMed:29100085}. Mitochondrion matrix, mitochondrion
CC nucleoid {ECO:0000269|PubMed:16825194, ECO:0000269|PubMed:18063578,
CC ECO:0000269|PubMed:25683715}. Note=Localizes to mitochondrial RNA
CC granules found in close proximity to the mitochondrial nucleoids
CC (PubMed:16825194, PubMed:25683715). Relocalizes to stress granules upon
CC heat stress (PubMed:29100085). {ECO:0000269|PubMed:16825194,
CC ECO:0000269|PubMed:25683715, ECO:0000269|PubMed:29100085}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q7L2E3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7L2E3-2; Sequence=VSP_022118;
CC Name=3;
CC IsoId=Q7L2E3-3; Sequence=VSP_036891, VSP_036892;
CC -!- PTM: [Isoform 2]: Phosphorylated on Ser-15.
CC {ECO:0007744|PubMed:18220336}.
CC -!- DISEASE: Neurodevelopmental disorder with severe motor impairment and
CC absent language (NEDMIAL) [MIM:617804]: An autosomal dominant
CC neurodevelopmental disorder characterized by global developmental
CC delay, intellectual disability, severe speech impairment and gait
CC abnormalities. {ECO:0000269|PubMed:28327206,
CC ECO:0000269|PubMed:29100085}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74913.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA92071.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AB020697; BAA74913.2; ALT_INIT; mRNA.
DR EMBL; AK002076; BAA92071.1; ALT_SEQ; mRNA.
DR EMBL; AK291266; BAF83955.1; -; mRNA.
DR EMBL; BC014237; AAH14237.1; -; mRNA.
DR EMBL; BC015029; AAH15029.1; -; mRNA.
DR EMBL; BC020126; AAH20126.1; -; mRNA.
DR EMBL; BC038417; AAH38417.1; -; mRNA.
DR CCDS; CCDS2759.1; -. [Q7L2E3-1]
DR PIR; E56236; E56236.
DR RefSeq; NP_055781.2; NM_014966.3. [Q7L2E3-3]
DR RefSeq; NP_619520.1; NM_138615.2. [Q7L2E3-1]
DR RefSeq; XP_011531796.1; XM_011533494.2. [Q7L2E3-1]
DR RefSeq; XP_011531797.1; XM_011533495.1. [Q7L2E3-1]
DR RefSeq; XP_016861406.1; XM_017005917.1. [Q7L2E3-3]
DR PDB; 2DB2; NMR; -; A=42-147.
DR PDBsum; 2DB2; -.
DR AlphaFoldDB; Q7L2E3; -.
DR SMR; Q7L2E3; -.
DR BioGRID; 116571; 458.
DR CORUM; Q7L2E3; -.
DR IntAct; Q7L2E3; 146.
DR MINT; Q7L2E3; -.
DR STRING; 9606.ENSP00000405620; -.
DR ChEMBL; CHEMBL4105814; -.
DR CarbonylDB; Q7L2E3; -.
DR GlyGen; Q7L2E3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7L2E3; -.
DR MetOSite; Q7L2E3; -.
DR PhosphoSitePlus; Q7L2E3; -.
DR SwissPalm; Q7L2E3; -.
DR BioMuta; DHX30; -.
DR DMDM; 74758997; -.
DR EPD; Q7L2E3; -.
DR jPOST; Q7L2E3; -.
DR MassIVE; Q7L2E3; -.
DR MaxQB; Q7L2E3; -.
DR PaxDb; Q7L2E3; -.
DR PeptideAtlas; Q7L2E3; -.
DR PRIDE; Q7L2E3; -.
DR ProteomicsDB; 68758; -. [Q7L2E3-1]
DR ProteomicsDB; 68759; -. [Q7L2E3-2]
DR ProteomicsDB; 68760; -. [Q7L2E3-3]
DR Antibodypedia; 13009; 173 antibodies from 23 providers.
DR DNASU; 22907; -.
DR Ensembl; ENST00000445061.6; ENSP00000405620.1; ENSG00000132153.15. [Q7L2E3-1]
DR Ensembl; ENST00000446256.6; ENSP00000392601.3; ENSG00000132153.15. [Q7L2E3-1]
DR Ensembl; ENST00000457607.1; ENSP00000394682.1; ENSG00000132153.15. [Q7L2E3-2]
DR Ensembl; ENST00000619982.4; ENSP00000483160.1; ENSG00000132153.15. [Q7L2E3-3]
DR GeneID; 22907; -.
DR KEGG; hsa:22907; -.
DR MANE-Select; ENST00000445061.6; ENSP00000405620.1; NM_138615.3; NP_619520.1.
DR UCSC; uc003cru.4; human. [Q7L2E3-1]
DR CTD; 22907; -.
DR DisGeNET; 22907; -.
DR GeneCards; DHX30; -.
DR HGNC; HGNC:16716; DHX30.
DR HPA; ENSG00000132153; Low tissue specificity.
DR MalaCards; DHX30; -.
DR MIM; 616423; gene.
DR MIM; 617804; phenotype.
DR neXtProt; NX_Q7L2E3; -.
DR OpenTargets; ENSG00000132153; -.
DR PharmGKB; PA27217; -.
DR VEuPathDB; HostDB:ENSG00000132153; -.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000158279; -.
DR HOGENOM; CLU_001832_1_2_1; -.
DR InParanoid; Q7L2E3; -.
DR OMA; QYSCTEH; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; Q7L2E3; -.
DR TreeFam; TF352030; -.
DR PathwayCommons; Q7L2E3; -.
DR SignaLink; Q7L2E3; -.
DR SIGNOR; Q7L2E3; -.
DR BioGRID-ORCS; 22907; 143 hits in 1088 CRISPR screens.
DR ChiTaRS; DHX30; human.
DR EvolutionaryTrace; Q7L2E3; -.
DR GenomeRNAi; 22907; -.
DR Pharos; Q7L2E3; Tchem.
DR PRO; PR:Q7L2E3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q7L2E3; protein.
DR Bgee; ENSG00000132153; Expressed in left testis and 173 other tissues.
DR ExpressionAtlas; Q7L2E3; baseline and differential.
DR Genevisible; Q7L2E3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0035770; C:ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; IMP:UniProtKB.
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; Alternative splicing; ATP-binding; Cytoplasm;
KW Disease variant; Helicase; Hydrolase; Intellectual disability;
KW Mitochondrion; Mitochondrion nucleoid; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..1194
FT /note="ATP-dependent RNA helicase DHX30"
FT /id="PRO_0000245538"
FT DOMAIN 53..121
FT /note="DRBM"
FT DOMAIN 444..612
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 654..827
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 559..562
FT /note="DEAH box"
FT BINDING 457..464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PU8"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..41
FT /note="MFSLDSFRKDRAQHRQRQCKLPPPRLPPMCVNPTPGGTISR -> MAAARRL
FT MALAAGISPRLQPLGPRAAGRQGRSRGFSSSCAHPDHTKEAAEAESGMAPGGPGEGDGS
FT LVN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022118"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_036891"
FT VAR_SEQ 40..41
FT /note="SR -> MA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_036892"
FT VARIANT 493
FT /note="R -> H (in NEDMIAL; changed localization to stress
FT granules; decreased RNA-binding; no effect on RNA-dependent
FT ATPase activity; by inducing the formation of stress
FT granules probably indirectly decreases global protein
FT synthesis; dbSNP:rs1057519436)"
FT /evidence="ECO:0000269|PubMed:28327206,
FT ECO:0000269|PubMed:29100085"
FT /id="VAR_080611"
FT VARIANT 562
FT /note="H -> R (in NEDMIAL; changed localization to stress
FT granules; decreased RNA-dependent ATPase activity; by
FT inducing the formation of stress granules probably
FT indirectly decreases global protein synthesis;
FT dbSNP:rs1060499733)"
FT /evidence="ECO:0000269|PubMed:28327206,
FT ECO:0000269|PubMed:29100085"
FT /id="VAR_080612"
FT VARIANT 781
FT /note="G -> D (in NEDMIAL; changed localization to stress
FT granules; decreased RNA-dependent ATPase activity; by
FT inducing the formation of stress granules probably
FT indirectly decreases global protein synthesis;
FT dbSNP:rs1553706775)"
FT /evidence="ECO:0000269|PubMed:29100085"
FT /id="VAR_080613"
FT VARIANT 782
FT /note="R -> W (in NEDMIAL; changed localization to stress
FT granules; decreased RNA-dependent ATPase activity; by
FT inducing the formation of stress granules probably
FT indirectly decreases global protein synthesis;
FT dbSNP:rs753242774)"
FT /evidence="ECO:0000269|PubMed:28327206,
FT ECO:0000269|PubMed:29100085"
FT /id="VAR_080614"
FT VARIANT 785
FT /note="R -> C (in NEDMIAL; changed localization to stress
FT granules; decreased RNA-dependent ATPase activity; by
FT inducing the formation of stress granules probably
FT indirectly decreases global protein synthesis;
FT dbSNP:rs1085307451)"
FT /evidence="ECO:0000269|PubMed:29100085"
FT /id="VAR_080615"
FT VARIANT 785
FT /note="R -> H (in NEDMIAL; changed localization to stress
FT granules; decreased RNA-dependent ATPase activity; by
FT inducing the formation of stress granules probably
FT indirectly decreases global protein synthesis;
FT dbSNP:rs1553706799)"
FT /evidence="ECO:0000269|PubMed:29100085"
FT /id="VAR_080616"
FT CONFLICT 557
FT /note="I -> T (in Ref. 2; BAF83955)"
FT /evidence="ECO:0000305"
FT CONFLICT 1136
FT /note="R -> W (in Ref. 3; AAH14237)"
FT /evidence="ECO:0000305"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2DB2"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:2DB2"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:2DB2"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:2DB2"
FT STRAND 81..91
FT /evidence="ECO:0007829|PDB:2DB2"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2DB2"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:2DB2"
FT HELIX 106..124
FT /evidence="ECO:0007829|PDB:2DB2"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:2DB2"
FT MOD_RES Q7L2E3-2:15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
SQ SEQUENCE 1194 AA; 133938 MW; 33D9A08799FE7A02 CRC64;
MFSLDSFRKD RAQHRQRQCK LPPPRLPPMC VNPTPGGTIS RASRDLLKEF PQPKNLLNSV
IGRALGISHA KDKLVYVHTN GPKKKKVTLH IKWPKSVEVE GYGSKKIDAE RQAAAAACQL
FKGWGLLGPR NELFDAAKYR VLADRFGSPA DSWWRPEPTM PPTSWRQLNP ESIRPGGPGG
LSRSLGREEE EDEEEELEEG TIDVTDFLSM TQQDSHAPLR DSRGSSFEMT DDDSAIRALT
QFPLPKNLLA KVIQIATSSS TAKNLMQFHT VGTKTKLSTL TLLWPCPMTF VAKGRRKAEA
ENKAAALACK KLKSLGLVDR NNEPLTHAMY NLASLRELGE TQRRPCTIQV PEPILRKIET
FLNHYPVESS WIAPELRLQS DDILPLGKDS GPLSDPITGK PYVPLLEAEE VRLSQSLLEL
WRRRGPVWQE APQLPVDPHR DTILNAIEQH PVVVISGDTG CGKTTRIPQL LLERYVTEGR
GARCNVIITQ PRRISAVSVA QRVSHELGPS LRRNVGFQVR LESKPPSRGG ALLFCTVGIL
LRKLQSNPSL EGVSHVIVDE VHERDVNTDF LLILLKGLQR LNPALRLVLM SATGDNERFS
RYFGGCPVIK VPGFMYPVKE HYLEDILAKL GKHQYLHRHR HHESEDECAL DLDLVTDLVL
HIDARGEPGG ILCFLPGWQE IKGVQQRLQE ALGMHESKYL ILPVHSNIPM MDQKAIFQQP
PVGVRKIVLA TNIAETSITI NDIVHVVDSG LHKEERYDLK TKVSCLETVW VSRANVIQRR
GRAGRCQSGF AYHLFPRSRL EKMVPFQVPE ILRTPLENLV LQAKIHMPEK TAVEFLSKAV
DSPNIKAVDE AVILLQEIGV LDQREYLTTL GQRLAHISTD PRLAKAIVLA AIFRCLHPLL
VVVSCLTRDP FSSSLQNRAE VDKVKALLSH DSGSDHLAFV RAVAGWEEVL RWQDRSSREN
YLEENLLYAP SLRFIHGLIK QFSENIYEAF LVGKPSDCTL ASAQCNEYSE EEELVKGVLM
AGLYPNLIQV RQGKVTRQGK FKPNSVTYRT KSGNILLHKS TINREATRLR SRWLTYFMAV
KSNGSVFVRD SSQVHPLAVL LLTDGDVHIR DDGRRATISL SDSDLLRLEG DSRTVRLLKE
LRRALGRMVE RSLRSELAAL PPSVQEEHGQ LLALLAELLR GPCGSFDVRK TADD
