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 27-MAR-2024, entry version 223. 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 FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RIGI ANF TRIM6, AND RP MUTAGENESIS OF SER-552 AND GLY-724. RX PubMed=35263596; DOI=10.1016/j.celrep.2022.110434; RA Hage A., Bharaj P., van Tol S., Giraldo M.I., Gonzalez-Orozco M., RA Valerdi K.M., Warren A.N., Aguilera-Aguirre L., Xie X., Widen S.G., RA Moulton H.M., Lee B., Johnson J.R., Krogan N.J., Garcia-Sastre A., RA Shi P.Y., Freiberg A.N., Rajsbaum R.; RT "The RNA helicase DHX16 recognizes specific viral RNA to trigger RIG-I- RT dependent innate antiviral immunity."; RL Cell Rep. 38:110434-110434(2022). RN [20] 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 [21] {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). RN [22] {ECO:0007744|PDB:7DVQ} RP STRUCTURE BY ELECTRON MICROSCOPY (2.89 ANGSTROMS), AND SUBUNIT. RX PubMed=33509932; DOI=10.1126/science.abg0879; RA Bai R., Wan R., Wang L., Xu K., Zhang Q., Lei J., Shi Y.; RT "Structure of the activated human minor spliceosome."; RL Science 371:0-0(2021). 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. As a CC component of the minor spliceosome, involved in the splicing of U12- CC type introns in pre-mRNAs (Probable). Plays also a role in innate CC antiviral response by acting as a pattern recognition receptor sensing CC splicing signals in viral RNA (PubMed:35263596). Mechanistically, TRIM6 CC promotes the interaction between unanchored 'Lys-48'-polyubiquitin CC chains and DHX16, leading to DHX16 interaction with RIGI and ssRNA to CC amplify RIGI-dependent innate antiviral immune responses CC (PubMed:35263596). {ECO:0000269|PubMed:20423332, CC ECO:0000269|PubMed:20841358, ECO:0000269|PubMed:25296192, CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:35263596, CC ECO:0000305|PubMed:33509932}. 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 Component of the minor spliceosome, which splices U12-type introns CC (PubMed:33509932). Interacts with GPKOW. Interacts with TRIM6 CC (PubMed:35263596). Interacts with RIGI (PubMed:35263596). CC {ECO:0000269|PubMed:20423332, ECO:0000269|PubMed:20841358, CC ECO:0000269|PubMed:25296192, ECO:0000269|PubMed:29360106, CC ECO:0000269|PubMed:33509932, ECO:0000269|PubMed:35263596}. 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}. Cytoplasm {ECO:0000269|PubMed:35263596}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 PDB; 7QTT; EM; 3.10 A; N=1-1041. DR PDB; 8CH6; EM; 5.90 A; N=1-1041. DR PDBsum; 5Z56; -. DR PDBsum; 5Z57; -. DR PDBsum; 5Z58; -. DR PDBsum; 6FF7; -. DR PDBsum; 7DVQ; -. DR PDBsum; 7QTT; -. DR PDBsum; 8CH6; -. DR AlphaFoldDB; O60231; -. DR EMDB; EMD-14146; -. DR EMDB; EMD-16658; -. DR EMDB; EMD-30875; -. DR EMDB; EMD-6889; -. DR EMDB; EMD-6890; -. DR EMDB; EMD-6891; -. DR SMR; O60231; -. DR BioGRID; 114027; 196. 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 SwissPalm; O60231; -. DR BioMuta; DHX16; -. DR EPD; O60231; -. DR jPOST; O60231; -. DR MassIVE; O60231; -. DR PaxDb; 9606-ENSP00000365625; -. DR PeptideAtlas; O60231; -. DR ProteomicsDB; 49258; -. DR Pumba; O60231; -. DR Antibodypedia; 26473; 115 antibodies from 25 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 AGR; HGNC:2739; -. 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; HITLMNV; -. DR OrthoDB; 5488182at2759; -. 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; 754 hits in 1170 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 97 other cell types or tissues. DR ExpressionAtlas; O60231; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProt. 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; IEA:RHEA. DR GO; GO:0004386; F:helicase activity; IBA:GO_Central. DR GO; GO:0060090; F:molecular adaptor activity; IDA:UniProt. DR GO; GO:0038187; F:pattern recognition receptor activity; IDA:UniProt. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003724; F:RNA helicase activity; TAS:Reactome. DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProt. DR GO; GO:0140374; P:antiviral innate immune response; IDA:UniProt. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc. DR CDD; cd17974; DEXHc_DHX16; 1. DR CDD; cd18791; SF2_C_RHA; 1. DR Gene3D; 1.20.120.1080; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR011709; DEAD-box_helicase_OB_fold. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS. DR InterPro; IPR048333; HA2_WH. DR InterPro; IPR007502; Helicase-assoc_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1. DR PANTHER; PTHR18934:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF21010; HA2_C; 1. DR Pfam; PF04408; HA2_N; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF07717; OB_NTP_bind; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00847; HA2; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR Genevisible; O60231; HS. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Disease variant; Helicase; Hydrolase; KW Immunity; Innate immunity; mRNA processing; mRNA splicing; Neuropathy; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW 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; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31256877" FT /id="VAR_083622" FT VARIANT 674 FT /note="T -> M (in NMOAS; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31256877" FT /id="VAR_083623" FT VARIANT 697 FT /note="Q -> H (in NMOAS; uncertain 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. Fails to interact with any of viral RNA FT forms." FT /evidence="ECO:0000269|PubMed:20423332, FT ECO:0000269|PubMed:25296192, ECO:0000269|PubMed:35263596" FT MUTAGEN 724 FT /note="G->N: Dominant-negative mutant. Impairs pre-mRNA FT splicing activity. Fails to interact with any of viral RNA FT forms." FT /evidence="ECO:0000269|PubMed:20423332, FT ECO:0000269|PubMed:20841358, ECO:0000269|PubMed:25296192, FT ECO:0000269|PubMed:35263596" 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 162..192 FT /evidence="ECO:0007829|PDB:7QTT" FT HELIX 223..255 FT /evidence="ECO:0007829|PDB:7QTT" FT HELIX 265..295 FT /evidence="ECO:0007829|PDB:7QTT" FT STRAND 305..307 FT /evidence="ECO:0007829|PDB:7QTT" FT HELIX 325..337 FT /evidence="ECO:0007829|PDB:7QTT" 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 636..639 FT /evidence="ECO:0007829|PDB:7QTT" FT STRAND 642..647 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 649..651 FT /evidence="ECO:0007829|PDB:7QTT" 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 STRAND 747..750 FT /evidence="ECO:0007829|PDB:7QTT" 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 TURN 799..801 FT /evidence="ECO:0007829|PDB:7QTT" 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 TURN 831..833 FT /evidence="ECO:0007829|PDB:7QTT" 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 889..893 FT /evidence="ECO:0007829|PDB:7QTT" 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 958..961 FT /evidence="ECO:0007829|PDB:7QTT" FT TURN 962..964 FT /evidence="ECO:0007829|PDB:7QTT" FT STRAND 977..979 FT /evidence="ECO:0007829|PDB:7QTT" 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 //