ID DHX15_HUMAN Reviewed; 795 AA. AC O43143; Q9NQT7; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2001, sequence version 2. DT 08-NOV-2023, entry version 220. DE RecName: Full=ATP-dependent RNA helicase DHX15 {ECO:0000305}; DE EC=3.6.4.13 {ECO:0000269|PubMed:19432882, ECO:0000269|PubMed:32179686}; DE AltName: Full=ATP-dependent RNA helicase #46; DE AltName: Full=DEAH box protein 15; DE AltName: Full=Splicing factor Prp43 {ECO:0000303|PubMed:12458796}; DE Short=hPrp43 {ECO:0000303|PubMed:12458796}; GN Name=DHX15 {ECO:0000303|PubMed:24990078, ECO:0000312|HGNC:HGNC:2738}; GN Synonyms=DBP1 {ECO:0000303|PubMed:9388478}, DDX15; 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], AND TISSUE SPECIFICITY. RX PubMed=9388478; DOI=10.1006/bbrc.1997.7585; RA Imamura O., Sugawara M., Furuichi Y.; RT "Cloning and characterization of a putative human RNA helicase gene of the RT DEAH-box protein family."; RL Biochem. Biophys. Res. Commun. 240:335-340(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SSB, AND SUBCELLULAR LOCATION. RC TISSUE=Placenta; RX PubMed=12458796; DOI=10.1017/s1355838202021076; RA Fouraux M.A., Kolkman M.J.M., Van der Heijden A., De Jong A.S., RA Van Venrooij W.J., Pruijn G.J.M.; RT "The human La (SS-B) autoantigen interacts with DDX15/hPrp43, a putative RT DEAH-box RNA helicase."; RL RNA 8:1428-1443(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; 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 IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [5] RP IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15146077; DOI=10.1261/rna.7320604; RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., RA Tuschl T., Luehrmann R.; RT "The human 18S U11/U12 snRNP contains a set of novel proteins not found in RT the U2-dependent spliceosome."; RL RNA 10:929-941(2004). RN [6] RP CATALYTIC ACTIVITY, AND INTERACTION WITH GPATCH2. RX PubMed=19432882; DOI=10.1111/j.1349-7006.2009.01185.x; RA Lin M.L., Fukukawa C., Park J.H., Naito K., Kijima K., Shimo A., Ajiro M., RA Nishidate T., Nakamura Y., Katagiri T.; RT "Involvement of G-patch domain containing 2 overexpression in breast RT carcinogenesis."; RL Cancer Sci. 100:1443-1450(2009). RN [7] RP FUNCTION, IDENTIFICATION IN THE INTRON LARGE COMPLEX, AND INTERACTION WITH RP TFIP11. RX PubMed=19103666; DOI=10.1093/nar/gkn1002; RA Yoshimoto R., Kataoka N., Okawa K., Ohno M.; RT "Isolation and characterization of post-splicing lariat-intron complexes."; RL Nucleic Acids Res. 37:891-902(2009). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-488, 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 [9] 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 [10] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=22002106; DOI=10.1074/mcp.m111.013680; RA Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.; RT "Systematic analysis of protein pools, isoforms, and modifications RT affecting turnover and subcellular localization."; RL Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY RP 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 [12] RP FUNCTION, RNA-BINDING, INTERACTION WITH MAVS, AND MUTAGENESIS OF LYS-166; RP THR-167; ASP-260 AND GLU-261. RX PubMed=24990078; DOI=10.4049/jimmunol.1303322; RA Lu H., Lu N., Weng L., Yuan B., Liu Y.J., Zhang Z.; RT "DHX15 senses double-stranded RNA in myeloid dendritic cells."; RL J. Immunol. 193:1364-1372(2014). 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, AND MUTAGENESIS OF LYS-166; THR-167; ASP-260 AND GLU-261. RX PubMed=24782566; DOI=10.1126/scisignal.2004841; RA Mosallanejad K., Sekine Y., Ishikura-Kinoshita S., Kumagai K., Nagano T., RA Matsuzawa A., Takeda K., Naguro I., Ichijo H.; RT "The DEAH-box RNA helicase DHX15 activates NF-kappaB and MAPK signaling RT downstream of MAVS during antiviral responses."; RL Sci. Signal. 7:ra40-ra40(2014). RN [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-786, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [16] RP FUNCTION, AND INTERACTION WITH NLRP6. RX PubMed=34161762; DOI=10.1016/j.celrep.2021.109205; RA Xing J., Zhou X., Fang M., Zhang E., Minze L.J., Zhang Z.; RT "DHX15 is required to control RNA virus-induced intestinal inflammation."; RL Cell Rep. 35:109205-109205(2021). RN [17] {ECO:0007744|PDB:5XDR} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 110-795. RX PubMed=28580923; DOI=10.1107/s2053230x17007336; RA Murakami K., Nakano K., Shimizu T., Ohto U.; RT "The crystal structure of human DEAH-box RNA helicase 15 reveals a domain RT organization of the mammalian DEAH/RHA family."; RL Acta Crystallogr. F Struct. Biol. Commun. 73:347-355(2017). RN [18] {ECO:0007744|PDB:6ID1} RP STRUCTURE BY ELECTRON MICROSCOPY (2.86 ANGSTROMS) OF MUTANT ALA-429 IN RP COMPLEX WITH THE INTRON LARGE COMPLEX, IDENTIFICATION IN THE INTRON LARGE RP COMPLEX, AND MUTAGENESIS OF THR-429. RX PubMed=30728453; DOI=10.1038/s41422-019-0143-x; RA Zhang X., Zhan X., Yan C., Zhang W., Liu D., Lei J., Shi Y.; RT "Structures of the human spliceosomes before and after release of the RT ligated exon."; RL Cell Res. 29:274-285(2019). RN [19] {ECO:0007744|PDB:6SH6, ECO:0007744|PDB:6SH7} RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 113-795 IN COMPLEX WITH NKRF, RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH NKRF, RP AND MUTAGENESIS OF PRO-327; TYR-485; ALA-489; VAL-523; PRO-533; LEU-536 AND RP LEU-540. RX PubMed=32179686; DOI=10.1073/pnas.1913880117; RA Studer M.K., Ivanovic L., Weber M.E., Marti S., Jonas S.; RT "Structural basis for DEAH-helicase activation by G-patch proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 117:7159-7170(2020). CC -!- FUNCTION: RNA helicase involved in mRNA processing and antiviral innate CC immunity (PubMed:19432882, PubMed:19103666, PubMed:32179686, CC PubMed:24990078, PubMed:24782566, PubMed:34161762). Pre-mRNA processing CC factor involved in disassembly of spliceosomes after the release of CC mature mRNA (PubMed:19103666). In cooperation with TFIP11 seem to be CC involved in the transition of the U2, U5 and U6 snRNP-containing IL CC complex to the snRNP-free IS complex leading to efficient debranching CC and turnover of excised introns (PubMed:19103666). Plays a key role in CC antiviral innate immunity by promoting both MAVS-dependent signaling CC and NLRP6 inflammasome (PubMed:24990078, PubMed:24782566, CC PubMed:34161762). Acts as an RNA virus sensor: recognizes and binds CC viral double stranded RNA (dsRNA) and activates the MAVS-dependent CC signaling to produce interferon-beta and interferon lambda-3 (IFNL3) CC (PubMed:24990078, PubMed:24782566, PubMed:34161762). Involved in CC intestinal antiviral innate immunity together with NLRP6: recognizes CC and binds viral dsRNA and promotes activation of the NLRP6 inflammasome CC in intestinal epithelial cells to restrict infection by enteric viruses CC (PubMed:34161762). The NLRP6 inflammasome acts by promoting maturation CC and secretion of IL18 in the extracellular milieu (PubMed:34161762). CC Also involved in antibacterial innate immunity by promoting Wnt-induced CC antimicrobial protein expression in Paneth cells (By similarity). CC {ECO:0000250|UniProtKB:O35286, ECO:0000269|PubMed:19103666, CC ECO:0000269|PubMed:19432882, ECO:0000269|PubMed:24782566, CC ECO:0000269|PubMed:24990078, ECO:0000269|PubMed:32179686, CC ECO:0000269|PubMed:34161762}. 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:19432882, ECO:0000269|PubMed:32179686}; CC -!- ACTIVITY REGULATION: ATPase activity is enhanced upon binding to G- CC patch domain-containing proteins (PubMed:32179686). G-patch domain- CC containing proteins act like a brace that tethers mobile sections of CC DHX15 together, stabilizing a functional conformation with high RNA CC affinity, thereby promoting the ATPase activity (PubMed:32179686). CC {ECO:0000269|PubMed:32179686}. CC -!- SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type CC spliceosome (PubMed:15146077). Identified in the Intron Large CC spliceosome complex (IL, also named intron lariat spliceosome), a post- CC mRNA release spliceosomal complex containing the excised intron, U2, U5 CC and U6 snRNPs, and splicing factors; the association may be transient CC (PubMed:19103666, PubMed:30728453). The IL complex exists in two CC distinct conformations, one with the DHX15 (ILS2) and one without CC (ILS1) (PubMed:30728453). Interacts with TFIP11 (via G-patch domain); CC indicative for a recruitment to the IL complex (PubMed:19103666). CC Interacts with SSB/La (PubMed:12458796). Interacts with GPATCH2 (via G- CC patch domain); promoting the RNA helicase activity (PubMed:19432882). CC Interacts with NKRF (via G-patch domain); promoting the RNA helicase CC activity (PubMed:32179686). Interacts with NLRP6 (PubMed:34161762). CC {ECO:0000269|PubMed:12458796, ECO:0000269|PubMed:15146077, CC ECO:0000269|PubMed:19103666, ECO:0000269|PubMed:19432882, CC ECO:0000269|PubMed:30728453, ECO:0000269|PubMed:32179686, CC ECO:0000269|PubMed:34161762}. CC -!- INTERACTION: CC O43143; Q8N302: AGGF1; NbExp=3; IntAct=EBI-1237044, EBI-747899; CC O43143; Q9P1Y5-2: CAMSAP3; NbExp=3; IntAct=EBI-1237044, EBI-18121830; CC O43143; P51114-2: FXR1; NbExp=3; IntAct=EBI-1237044, EBI-11022345; CC O43143; O95872: GPANK1; NbExp=3; IntAct=EBI-1237044, EBI-751540; CC O43143; O95678: KRT75; NbExp=3; IntAct=EBI-1237044, EBI-2949715; CC O43143; O15226: NKRF; NbExp=4; IntAct=EBI-1237044, EBI-766011; CC O43143; Q96RS6-1: NUDCD1; NbExp=2; IntAct=EBI-1237044, EBI-20724008; CC O43143; P98175: RBM10; NbExp=3; IntAct=EBI-1237044, EBI-721525; CC O43143; Q96I25: RBM17; NbExp=11; IntAct=EBI-1237044, EBI-740272; CC O43143; P52756: RBM5; NbExp=15; IntAct=EBI-1237044, EBI-714003; CC O43143; Q15428: SF3A2; NbExp=2; IntAct=EBI-1237044, EBI-2462271; CC O43143; Q8IWZ8: SUGP1; NbExp=2; IntAct=EBI-1237044, EBI-2691671; CC O43143; A0A0S2Z6H0: ZGPAT; NbExp=3; IntAct=EBI-1237044, EBI-16428984; CC O43143; Q8N5A5: ZGPAT; NbExp=6; IntAct=EBI-1237044, EBI-3439227; CC O43143; Q8N5A5-2: ZGPAT; NbExp=12; IntAct=EBI-1237044, EBI-10183064; CC O43143; Q91WS2-1: Nlrp6; Xeno; NbExp=2; IntAct=EBI-1237044, EBI-16182226; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12458796}. Nucleus, CC nucleolus {ECO:0000269|PubMed:12458796}. CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9388478}. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily. CC DDX15/PRP43 sub-subfamily. {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; AB001636; BAA23987.1; -; mRNA. DR EMBL; AF279891; AAF90182.1; -; mRNA. DR EMBL; BC035974; AAH35974.1; -; mRNA. DR CCDS; CCDS33966.1; -. DR PIR; JC5785; JC5785. DR RefSeq; NP_001349.2; NM_001358.2. DR PDB; 5XDR; X-ray; 2.00 A; A=110-795. DR PDB; 6ID1; EM; 2.86 A; V=1-795. DR PDB; 6SH6; X-ray; 1.85 A; A=113-795. DR PDB; 6SH7; X-ray; 2.21 A; A=113-795. DR PDB; 8EJM; X-ray; 1.80 A; A=113-795. DR PDBsum; 5XDR; -. DR PDBsum; 6ID1; -. DR PDBsum; 6SH6; -. DR PDBsum; 6SH7; -. DR PDBsum; 8EJM; -. DR AlphaFoldDB; O43143; -. DR SMR; O43143; -. DR BioGRID; 108029; 472. DR CORUM; O43143; -. DR DIP; DIP-38211N; -. DR IntAct; O43143; 123. DR MINT; O43143; -. DR STRING; 9606.ENSP00000336741; -. DR ChEMBL; CHEMBL4295661; -. DR GlyCosmos; O43143; 3 sites, 1 glycan. DR GlyGen; O43143; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; O43143; -. DR MetOSite; O43143; -. DR PhosphoSitePlus; O43143; -. DR SwissPalm; O43143; -. DR BioMuta; DHX15; -. DR SWISS-2DPAGE; O43143; -. DR EPD; O43143; -. DR jPOST; O43143; -. DR MassIVE; O43143; -. DR MaxQB; O43143; -. DR PaxDb; 9606-ENSP00000336741; -. DR PeptideAtlas; O43143; -. DR ProteomicsDB; 48760; -. DR Pumba; O43143; -. DR Antibodypedia; 10152; 186 antibodies from 22 providers. DR DNASU; 1665; -. DR Ensembl; ENST00000336812.5; ENSP00000336741.4; ENSG00000109606.13. DR GeneID; 1665; -. DR KEGG; hsa:1665; -. DR MANE-Select; ENST00000336812.5; ENSP00000336741.4; NM_001358.3; NP_001349.2. DR UCSC; uc003gqx.4; human. DR AGR; HGNC:2738; -. DR CTD; 1665; -. DR DisGeNET; 1665; -. DR GeneCards; DHX15; -. DR HGNC; HGNC:2738; DHX15. DR HPA; ENSG00000109606; Low tissue specificity. DR MIM; 603403; gene. DR neXtProt; NX_O43143; -. DR OpenTargets; ENSG00000109606; -. DR PharmGKB; PA27204; -. DR VEuPathDB; HostDB:ENSG00000109606; -. DR eggNOG; KOG0925; Eukaryota. DR GeneTree; ENSGT00940000155800; -. DR HOGENOM; CLU_001832_5_11_1; -. DR InParanoid; O43143; -. DR OMA; MKVYPLY; -. DR OrthoDB; 5488182at2759; -. DR PhylomeDB; O43143; -. DR TreeFam; TF105735; -. DR PathwayCommons; O43143; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; O43143; -. DR BioGRID-ORCS; 1665; 840 hits in 1166 CRISPR screens. DR ChiTaRS; DHX15; human. DR GeneWiki; DHX15; -. DR GenomeRNAi; 1665; -. DR Pharos; O43143; Tbio. DR PRO; PR:O43143; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; O43143; Protein. DR Bgee; ENSG00000109606; Expressed in cartilage tissue and 201 other tissues. DR Genevisible; O43143; HS. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central. DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:HGNC-UCL. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; TAS:Reactome. DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB. DR GO; GO:0004386; F:helicase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB. DR GO; GO:0140374; P:antiviral innate immune response; IDA:UniProtKB. DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IDA:UniProtKB. DR GO; GO:0043279; P:response to alkaloid; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl. DR GO; GO:0008380; P:RNA splicing; IC:HGNC-UCL. DR CDD; cd17973; DEXHc_DHX15; 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; IPR044756; DHX15_DEXHc. 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 PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1. DR PANTHER; PTHR18934:SF95; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX15; 1. 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; 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. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Helicase; Hydrolase; Immunity; KW Innate immunity; Isopeptide bond; mRNA processing; mRNA splicing; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW RNA-binding; Ubl conjugation. FT CHAIN 1..795 FT /note="ATP-dependent RNA helicase DHX15" FT /id="PRO_0000055139" FT DOMAIN 147..313 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 338..518 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 1..108 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 260..263 FT /note="DEAH box" FT COMPBIAS 1..63 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 81..108 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 160..167 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 488 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 786 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT MUTAGEN 166 FT /note="K->A: Abolished ATPase activity without affecting FT ability to activate the MAVS-dependent signaling to produce FT interferon-beta." FT /evidence="ECO:0000269|PubMed:24782566, FT ECO:0000269|PubMed:24990078" FT MUTAGEN 167 FT /note="T->A: Abolished ATPase activity without affecting FT ability to activate the MAVS-dependent signaling to produce FT interferon-beta." FT /evidence="ECO:0000269|PubMed:24782566, FT ECO:0000269|PubMed:24990078" FT MUTAGEN 260 FT /note="D->A: Abolished ATPase activity without affecting FT ability to activate the MAVS-dependent signaling to produce FT interferon-beta." FT /evidence="ECO:0000269|PubMed:24782566, FT ECO:0000269|PubMed:24990078" FT MUTAGEN 261 FT /note="E->A: Abolished ATPase activity without affecting FT ability to activate the MAVS-dependent signaling to produce FT interferon-beta." FT /evidence="ECO:0000269|PubMed:24782566, FT ECO:0000269|PubMed:24990078" FT MUTAGEN 327 FT /note="P->E: Abolished interaction with NKRF." FT /evidence="ECO:0000269|PubMed:32179686" FT MUTAGEN 429 FT /note="T->A: Abolished ATPase activity." FT /evidence="ECO:0000269|PubMed:30728453" FT MUTAGEN 485 FT /note="Y->E: Abolished interaction with NKRF." FT /evidence="ECO:0000269|PubMed:32179686" FT MUTAGEN 489 FT /note="A->E: Decreased, but not abolished interaction, with FT NKRF." FT /evidence="ECO:0000269|PubMed:32179686" FT MUTAGEN 523 FT /note="V->E: Abolished interaction with NKRF." FT /evidence="ECO:0000269|PubMed:32179686" FT MUTAGEN 533 FT /note="P->E: Abolished interaction with NKRF." FT /evidence="ECO:0000269|PubMed:32179686" FT MUTAGEN 536 FT /note="L->E: Abolished interaction with NKRF." FT /evidence="ECO:0000269|PubMed:32179686" FT MUTAGEN 540 FT /note="L->E: Abolished interaction with NKRF." FT /evidence="ECO:0000269|PubMed:32179686" FT CONFLICT 151 FT /note="V -> G (in Ref. 1; BAA23987)" FT /evidence="ECO:0000305" FT CONFLICT 172..173 FT /note="QW -> HR (in Ref. 1; BAA23987)" FT /evidence="ECO:0000305" FT CONFLICT 232..234 FT /note="ILK -> FFM (in Ref. 1; BAA23987)" FT /evidence="ECO:0000305" FT CONFLICT 786..795 FT /note="KLQSKEYSQY -> QTSIQGIFTVLNSVLRTEVIERTALKDE (in Ref. FT 1; BAA23987)" FT /evidence="ECO:0000305" FT STRAND 114..116 FT /evidence="ECO:0007829|PDB:6SH6" FT TURN 117..120 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 125..134 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 138..142 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 143..150 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 154..159 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 166..179 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:5XDR" FT STRAND 187..193 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 195..208 FT /evidence="ECO:0007829|PDB:6SH6" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 224..226 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 233..237 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 238..245 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 254..259 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 262..264 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 267..282 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 287..294 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 296..298 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 299..303 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 319..323 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 331..345 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 351..355 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 359..374 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 378..380 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 383..388 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 394..397 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 398..401 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 409..412 FT /evidence="ECO:0007829|PDB:5XDR" FT STRAND 415..420 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 423..426 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 433..438 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 441..448 FT /evidence="ECO:0007829|PDB:6SH6" FT TURN 449..452 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 453..460 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 463..471 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 472..474 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 475..485 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 487..493 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 501..503 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 508..516 FT /evidence="ECO:0007829|PDB:6SH6" FT TURN 522..524 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 533..545 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 557..563 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 565..567 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 569..578 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 579..581 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 584..594 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 604..606 FT /evidence="ECO:0007829|PDB:5XDR" FT HELIX 607..615 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 623..636 FT /evidence="ECO:0007829|PDB:6SH6" FT TURN 637..639 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 641..646 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 651..670 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 684..697 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 700..704 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 710..712 FT /evidence="ECO:0007829|PDB:6SH6" FT TURN 713..715 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 718..721 FT /evidence="ECO:0007829|PDB:6SH6" FT STRAND 732..752 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 755..761 FT /evidence="ECO:0007829|PDB:6SH6" FT TURN 763..765 FT /evidence="ECO:0007829|PDB:6SH6" FT TURN 768..770 FT /evidence="ECO:0007829|PDB:6SH6" FT HELIX 775..788 FT /evidence="ECO:0007829|PDB:6SH6" SQ SEQUENCE 795 AA; 90933 MW; 9A21FBE0051CCAA9 CRC64; MSKRHRLDLG EDYPSGKKRA GTDGKDRDRD RDREDRSKDR DRERDRGDRE REREKEKEKE LRASTNAMLI SAGLPPLKAS HSAHSTHSAH STHSTHSAHS THAGHAGHTS LPQCINPFTN LPHTPRYYDI LKKRLQLPVW EYKDRFTDIL VRHQSFVLVG ETGSGKTTQI PQWCVEYMRS LPGPKRGVAC TQPRRVAAMS VAQRVADEMD VMLGQEVGYS IRFEDCSSAK TILKYMTDGM LLREAMNDPL LERYGVIILD EAHERTLATD ILMGVLKEVV RQRSDLKVIV MSATLDAGKF QIYFDNCPLL TIPGRTHPVE IFYTPEPERD YLEAAIRTVI QIHMCEEEEG DLLLFLTGQE EIDEACKRIK REVDDLGPEV GDIKIIPLYS TLPPQQQQRI FEPPPPKKQN GAIGRKVVVS TNIAETSLTI DGVVFVIDPG FAKQKVYNPR IRVESLLVTA ISKASAQQRA GRAGRTRPGK CFRLYTEKAY KTEMQDNTYP EILRSNLGSV VLQLKKLGID DLVHFDFMDP PAPETLMRAL ELLNYLAALN DDGDLTELGS MMAEFPLDPQ LAKMVIASCD YNCSNEVLSI TAMLSVPQCF VRPTEAKKAA DEAKMRFAHI DGDHLTLLNV YHAFKQNHES VQWCYDNFIN YRSLMSADNV RQQLSRIMDR FNLPRRSTDF TSRDYYINIR KALVTGYFMQ VAHLERTGHY LTVKDNQVVQ LHPSTVLDHK PEWVLYNEFV LTTKNYIRTC TDIKPEWLVK IAPQYYDMSN FPQCEAKRQL DRIIAKLQSK EYSQY //