DHX15_HUMAN
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 03-AUG-2022, entry version 213.
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}.
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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 PDBsum; 5XDR; -.
DR PDBsum; 6ID1; -.
DR PDBsum; 6SH6; -.
DR PDBsum; 6SH7; -.
DR AlphaFoldDB; O43143; -.
DR SMR; O43143; -.
DR BioGRID; 108029; 328.
DR CORUM; O43143; -.
DR DIP; DIP-38211N; -.
DR IntAct; O43143; 118.
DR MINT; O43143; -.
DR STRING; 9606.ENSP00000336741; -.
DR ChEMBL; CHEMBL4295661; -.
DR GlyGen; O43143; 3 sites, 1 O-linked glycan (3 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; O43143; -.
DR PeptideAtlas; O43143; -.
DR PRIDE; O43143; -.
DR ProteomicsDB; 48760; -.
DR Antibodypedia; 10152; 180 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 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; DHDLKRY; -.
DR OrthoDB; 354219at2759; -.
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; 802 hits in 1082 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:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
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:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; 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 Gene3D; 3.40.50.300; -; 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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; 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
