DHX16_HUMAN
ID DHX16_HUMAN Reviewed; 1041 AA.
AC O60231; O60322; Q5JP45; Q969X7; Q96QC1;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase #3;
DE AltName: Full=DEAH-box protein 16;
GN Name=DHX16;
GN Synonyms=DBP2, DDX16, KIAA0577, PRP2 {ECO:0000303|PubMed:20841358,
GN ECO:0000303|PubMed:25296192};
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].
RX PubMed=9547260; DOI=10.1093/nar/26.9.2063;
RA Imamura O., Saiki K., Tani T., Ohshima Y., Sugawara M., Furuichi Y.;
RT "Cloning and characterization of a human DEAH-box RNA helicase, a
RT functional homolog of fission yeast Cdc28/Prp8.";
RL Nucleic Acids Res. 26:2063-2068(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-566.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-160, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-106 AND SER-107, AND
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND IDENTIFICATION BY
RP 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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-428; ASP-520;
RP HIS-523; SER-552 AND GLY-724.
RX PubMed=20423332; DOI=10.1042/bj20100266;
RA Gencheva M., Kato M., Newo A.N., Lin R.J.;
RT "Contribution of DEAH-box protein DHX16 in human pre-mRNA splicing.";
RL Biochem. J. 429:25-32(2010).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-724.
RX PubMed=20841358; DOI=10.1074/jbc.m110.122309;
RA Gencheva M., Lin T.Y., Wu X., Yang L., Richard C., Jones M., Lin S.B.,
RA Lin R.J.;
RT "Nuclear retention of unspliced pre-mRNAs by mutant DHX16/hPRP2, a
RT spliceosomal DEAH-box protein.";
RL J. Biol. Chem. 285:35624-35632(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-106; SER-107 AND
RP SER-160, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-107, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-106; SER-160 AND
RP THR-712, AND 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 [18]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GPKOW, AND MUTAGENESIS OF
RP SER-552 AND GLY-724.
RX PubMed=25296192; DOI=10.1042/bsr20140142;
RA Zang S., Lin T.Y., Chen X., Gencheva M., Newo A.N., Yang L., Rossi D.,
RA Hu J., Lin S.B., Huang A., Lin R.J.;
RT "GPKOW is essential for pre-mRNA splicing in vitro and suppresses splicing
RT defect caused by dominant-negative DHX16 mutation in vivo.";
RL Biosci. Rep. 34:E00163-E00163(2014).
RN [19]
RP INVOLVEMENT IN NMOAS, VARIANTS NMOAS GLU-427; ILE-582; MET-674 AND HIS-697,
RP AND TISSUE SPECIFICITY.
RX PubMed=31256877; DOI=10.1016/j.ajhg.2019.06.001;
RG University of Washington Center for Mendelian Genomics, Baylor-Hopkins Center for Mendelian Genomics, Telethon Undiagnosed Diseases Program;
RA Paine I., Posey J.E., Grochowski C.M., Jhangiani S.N., Rosenheck S.,
RA Kleyner R., Marmorale T., Yoon M., Wang K., Robison R., Cappuccio G.,
RA Pinelli M., Magli A., Coban Akdemir Z., Hui J., Yeung W.L., Wong B.K.Y.,
RA Ortega L., Bekheirnia M.R., Bierhals T., Hempel M., Johannsen J.,
RA Santer R., Aktas D., Alikasifoglu M., Bozdogan S., Aydin H., Karaca E.,
RA Bayram Y., Ityel H., Dorschner M., White J.J., Wilichowski E.,
RA Wortmann S.B., Casella E.B., Kitajima J.P., Kok F., Monteiro F.,
RA Muzny D.M., Bamshad M., Gibbs R.A., Sutton V.R., Van Esch H.,
RA Brunetti-Pierri N., Hildebrandt F., Brautbar A., Van den Veyver I.B.,
RA Glass I., Lessel D., Lyon G.J., Lupski J.R.;
RT "Paralog studies augment gene discovery: DDX and DHX genes.";
RL Am. J. Hum. Genet. 105:302-316(2019).
RN [20] {ECO:0007744|PDB:5Z56, ECO:0007744|PDB:5Z57, ECO:0007744|PDB:5Z58}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=29360106; DOI=10.1038/cr.2018.14;
RA Zhang X., Yan C., Zhan X., Li L., Lei J., Shi Y.;
RT "Structure of the human activated spliceosome in three conformational
RT states.";
RL Cell Res. 28:307-322(2018).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome (PubMed:20423332, PubMed:20841358, PubMed:25296192,
CC PubMed:29360106). Contributes to pre-mRNA splicing after spliceosome
CC formation and prior to the first transesterification reaction.
CC {ECO:0000269|PubMed:20423332, ECO:0000269|PubMed:20841358,
CC ECO:0000269|PubMed:25296192, ECO:0000269|PubMed:29360106}.
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 -!- SUBUNIT: Component of pre-catalytic spliceosome complexes
CC (PubMed:20423332, PubMed:20841358, PubMed:25296192, PubMed:29360106).
CC Interacts with GPKOW. {ECO:0000269|PubMed:20423332,
CC ECO:0000269|PubMed:20841358, ECO:0000269|PubMed:25296192,
CC ECO:0000269|PubMed:29360106}.
CC -!- INTERACTION:
CC O60231; Q92620: DHX38; NbExp=2; IntAct=EBI-311446, EBI-1043041;
CC O60231; Q92917: GPKOW; NbExp=3; IntAct=EBI-311446, EBI-746309;
CC O60231; Q13435: SF3B2; NbExp=2; IntAct=EBI-311446, EBI-749111;
CC O60231; Q9HCS7: XAB2; NbExp=2; IntAct=EBI-311446, EBI-295232;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20423332,
CC ECO:0000269|PubMed:20841358, ECO:0000269|PubMed:25296192,
CC ECO:0000269|PubMed:29360106}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:20423332}.
CC -!- TISSUE SPECIFICITY: Expressed in the spleen, thyroid and testis. Also
CC expressed in the brain and cerebellum. {ECO:0000269|PubMed:31256877}.
CC -!- DISEASE: Neuromuscular oculoauditory syndrome (NMOAS) [MIM:618733]: An
CC autosomal dominant neuromuscular disorder characterized by variable
CC features including myopathy, neuropathy, hypotonia, joint contractures,
CC growth delay, chorioretinal lacunae, sensorineuronal deafness, agenesis
CC of the corpus callosum, and seizures. {ECO:0000269|PubMed:31256877}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX16/PRP8 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25503.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB001601; BAA25908.1; -; mRNA.
DR EMBL; BA000025; BAB63323.1; -; Genomic_DNA.
DR EMBL; AB011149; BAA25503.2; ALT_INIT; mRNA.
DR EMBL; AL845353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008825; AAH08825.1; -; mRNA.
DR EMBL; BC009392; AAH09392.1; -; mRNA.
DR CCDS; CCDS4685.1; -.
DR RefSeq; NP_001157711.1; NM_001164239.1.
DR RefSeq; NP_003578.2; NM_003587.4.
DR PDB; 5Z56; EM; 5.10 A; x=1-1041.
DR PDB; 5Z57; EM; 6.50 A; x=1-1041.
DR PDB; 5Z58; EM; 4.90 A; x=1-1041.
DR PDB; 6FF7; EM; 4.50 A; q=1-1041.
DR PDB; 7DVQ; EM; 2.89 A; x=1-1041.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 5Z58; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 7DVQ; -.
DR AlphaFoldDB; O60231; -.
DR SMR; O60231; -.
DR BioGRID; 114027; 164.
DR CORUM; O60231; -.
DR IntAct; O60231; 35.
DR MINT; O60231; -.
DR STRING; 9606.ENSP00000365625; -.
DR GlyGen; O60231; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60231; -.
DR MetOSite; O60231; -.
DR PhosphoSitePlus; O60231; -.
DR BioMuta; DHX16; -.
DR EPD; O60231; -.
DR jPOST; O60231; -.
DR MassIVE; O60231; -.
DR PaxDb; O60231; -.
DR PeptideAtlas; O60231; -.
DR PRIDE; O60231; -.
DR ProteomicsDB; 49258; -.
DR Antibodypedia; 26473; 102 antibodies from 24 providers.
DR DNASU; 8449; -.
DR Ensembl; ENST00000376442.8; ENSP00000365625.3; ENSG00000204560.10.
DR Ensembl; ENST00000383577.8; ENSP00000373071.4; ENSG00000206486.8.
DR Ensembl; ENST00000417308.6; ENSP00000390938.2; ENSG00000233561.6.
DR Ensembl; ENST00000421095.6; ENSP00000396193.2; ENSG00000226171.6.
DR Ensembl; ENST00000424672.6; ENSP00000389862.2; ENSG00000233418.8.
DR Ensembl; ENST00000451456.6; ENSP00000408956.2; ENSG00000233049.6.
DR Ensembl; ENST00000458094.6; ENSP00000393958.2; ENSG00000231377.6.
DR GeneID; 8449; -.
DR KEGG; hsa:8449; -.
DR MANE-Select; ENST00000376442.8; ENSP00000365625.3; NM_003587.5; NP_003578.2.
DR UCSC; uc011ijv.3; human.
DR CTD; 8449; -.
DR DisGeNET; 8449; -.
DR GeneCards; DHX16; -.
DR HGNC; HGNC:2739; DHX16.
DR HPA; ENSG00000204560; Low tissue specificity.
DR MalaCards; DHX16; -.
DR MIM; 603405; gene.
DR MIM; 618733; phenotype.
DR neXtProt; NX_O60231; -.
DR OpenTargets; ENSG00000204560; -.
DR PharmGKB; PA27205; -.
DR VEuPathDB; HostDB:ENSG00000204560; -.
DR eggNOG; KOG0923; Eukaryota.
DR GeneTree; ENSGT00940000158480; -.
DR HOGENOM; CLU_001832_7_1_1; -.
DR InParanoid; O60231; -.
DR OMA; PHYHKKK; -.
DR OrthoDB; 354219at2759; -.
DR PhylomeDB; O60231; -.
DR TreeFam; TF313473; -.
DR BRENDA; 3.6.4.13; 2681.
DR PathwayCommons; O60231; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; O60231; -.
DR SIGNOR; O60231; -.
DR BioGRID-ORCS; 8449; 729 hits in 1091 CRISPR screens.
DR GeneWiki; DHX16; -.
DR GenomeRNAi; 8449; -.
DR Pharos; O60231; Tbio.
DR PRO; PR:O60231; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O60231; protein.
DR Bgee; ENSG00000204560; Expressed in sural nerve and 95 other tissues.
DR ExpressionAtlas; O60231; baseline and differential.
DR Genevisible; O60231; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; EXP:Reactome.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
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; ATP-binding; Disease variant; Helicase; Hydrolase;
KW mRNA processing; mRNA splicing; Neuropathy; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome.
FT CHAIN 1..1041
FT /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase
FT DHX16"
FT /id="PRO_0000055151"
FT DOMAIN 409..573
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 598..771
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 101..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 520..523
FT /note="DEAH box"
FT COMPBIAS 130..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 422..429
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 712
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 352
FT /note="K -> E (in dbSNP:rs17189239)"
FT /id="VAR_057236"
FT VARIANT 427
FT /note="G -> E (in NMOAS)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083621"
FT VARIANT 502
FT /note="L -> F (in dbSNP:rs17189232)"
FT /id="VAR_057237"
FT VARIANT 566
FT /note="D -> G (in dbSNP:rs9262138)"
FT /evidence="ECO:0000269|PubMed:14574404"
FT /id="VAR_057238"
FT VARIANT 582
FT /note="F -> I (in NMOAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083622"
FT VARIANT 674
FT /note="T -> M (in NMOAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083623"
FT VARIANT 697
FT /note="Q -> H (in NMOAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083624"
FT MUTAGEN 428
FT /note="K->A: Impairs pre-mRNA splicing activity."
FT /evidence="ECO:0000269|PubMed:20423332"
FT MUTAGEN 520
FT /note="D->A: Impairs pre-mRNA splicing activity."
FT /evidence="ECO:0000269|PubMed:20423332"
FT MUTAGEN 523
FT /note="H->A: No loss of pre-mRNA splicing activity."
FT /evidence="ECO:0000269|PubMed:20423332"
FT MUTAGEN 552
FT /note="S->L: Dominant-negative mutant. Impairs pre-mRNA
FT splicing activity."
FT /evidence="ECO:0000269|PubMed:20423332,
FT ECO:0000269|PubMed:25296192"
FT MUTAGEN 724
FT /note="G->N: Dominant-negative mutant. Impairs pre-mRNA
FT splicing activity."
FT /evidence="ECO:0000269|PubMed:20423332,
FT ECO:0000269|PubMed:20841358, ECO:0000269|PubMed:25296192"
FT CONFLICT 223
FT /note="V -> I (in Ref. 1; BAA25908)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="R -> P (in Ref. 1; BAA25908)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="L -> P (in Ref. 1; BAA25908)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="A -> T (in Ref. 1; BAA25908)"
FT /evidence="ECO:0000305"
FT CONFLICT 899
FT /note="Y -> C (in Ref. 1; BAA25908)"
FT /evidence="ECO:0000305"
FT CONFLICT 1032
FT /note="K -> KK (in Ref. 5; AAH08825/AAH09392)"
FT /evidence="ECO:0000305"
FT HELIX 387..395
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 401..414
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 416..421
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 428..439
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 455..468
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 477..481
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 493..497
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 498..507
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 515..520
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 527..542
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 547..555
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 558..563
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 579..583
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 592..605
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 610..614
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 618..635
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 642..647
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 653..656
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 657..660
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 668..673
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 676..679
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 686..691
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 694..701
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 702..705
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 706..713
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 716..722
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 723..727
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 728..730
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 732..738
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 740..744
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 754..756
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 761..767
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 768..771
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 775..777
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 786..798
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 810..815
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 818..820
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 822..830
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 837..847
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 866..871
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 878..888
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 899..902
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 905..924
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 935..946
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 947..949
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 950..953
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 984..1002
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 1005..1011
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 1013..1016
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 1037..1039
FT /evidence="ECO:0007829|PDB:7DVQ"
SQ SEQUENCE 1041 AA; 119264 MW; 5CAC4DBEF21A4E6D CRC64;
MATPAGLERW VQDELHSVLG LSERHVAQFL IGTAQRCTSA EEFVQRLRDT DTLDLSGPAR
DFALRLWNKV PRKAVVEKPA RAAEREARAL LEKNRSYRLL EDSEESSEET VSRAGSSLQK
KRKKRKHLRK KREEEEEEEA SEKGKKKTGG SKQQTEKPES EDEWERTERE RLQDLEERDA
FAERVRQRDK DRTRNVLERS DKKAYEEAQK RLKMAEEDRK AMVPELRKKS RREYLAKRER
EKLEDLEAEL ADEEFLFGDV ELSRHERQEL KYKRRVRDLA REYRAAGEQE KLEATNRYHM
PKETRGQPAR AVDLVEEESG APGEEQRRWE EARLGAASLK FGARDAASQE PKYQLVLEEE
ETIEFVRATQ LQGDEEPSAP PTSTQAQQKE SIQAVRRSLP VFPFREELLA AIANHQVLII
EGETGSGKTT QIPQYLFEEG YTNKGMKIAC TQPRRVAAMS VAARVAREMG VKLGNEVGYS
IRFEDCTSER TVLRYMTDGM LLREFLSEPD LASYSVVMVD EAHERTLHTD ILFGLIKDVA
RFRPELKVLV ASATMDTARF STFFDDAPVF RIPGRRFPVD IFYTKAPEAD YLEACVVSVL
QIHVTQPPGD ILVFLTGQEE IEAACEMLQD RCRRLGSKIR ELLVLPIYAN LPSDMQARIF
QPTPPGARKV VVATNIAETS LTIEGIIYVL DPGFCKQKSY NPRTGMESLT VTPCSKASAN
QRAGRAGRVA AGKCFRLYTA WAYQHELEET TVPEIQRTSL GNVVLLLKSL GIHDLMHFDF
LDPPPYETLL LALEQLYALG ALNHLGELTT SGRKMAELPV DPMLSKMILA SEKYSCSEEI
LTVAAMLSVN NSIFYRPKDK VVHADNARVN FFLPGGDHLV LLNVYTQWAE SGYSSQWCYE
NFVQFRSMRR ARDVREQLEG LLERVEVGLS SCQGDYIRVR KAITAGYFYH TARLTRSGYR
TVKQQQTVFI HPNSSLFEQQ PRWLLYHELV LTTKEFMRQV LEIESSWLLE VAPHYYKAKE
LEDPHAKKMP KKIGKTREEL G
