DHX9_BOVIN
ID DHX9_BOVIN Reviewed; 1287 AA.
AC Q28141;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=ATP-dependent RNA helicase A {ECO:0000250|UniProtKB:Q08211};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q08211};
DE AltName: Full=DEAH box protein 9 {ECO:0000250|UniProtKB:O70133};
DE AltName: Full=Nuclear DNA helicase II {ECO:0000250|UniProtKB:Q08211};
DE Short=NDH II {ECO:0000250|UniProtKB:Q08211};
GN Name=DHX9 {ECO:0000250|UniProtKB:Q08211};
GN Synonyms=DDX9 {ECO:0000250|UniProtKB:Q08211}, NDH2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=7608213; DOI=10.1074/jbc.270.27.16422;
RA Zhang S., Maacke H., Grosse F.;
RT "Molecular cloning of the gene encoding nuclear DNA helicase II. A bovine
RT homologue of human RNA helicase A and Drosophila Mle protein.";
RL J. Biol. Chem. 270:16422-16427(1995).
RN [2]
RP FUNCTION AS AN ATP-DEPENDENT HELICASE, DNA-BINDING, AND RNA-BINDING.
RX PubMed=7511411; DOI=10.1021/bi00179a016;
RA Zhang S., Grosse F.;
RT "Nuclear DNA helicase II unwinds both DNA and RNA.";
RL Biochemistry 33:3906-3912(1994).
CC -!- FUNCTION: Multifunctional ATP-dependent nucleic acid helicase that
CC unwinds DNA and RNA in a 3' to 5' direction and that plays important
CC roles in many processes, such as DNA replication, transcriptional
CC activation, post-transcriptional RNA regulation, mRNA translation and
CC RNA-mediated gene silencing (PubMed:7511411). Requires a 3'-single-
CC stranded tail as entry site for acid nuclei unwinding activities as
CC well as the binding and hydrolyzing of any of the four ribo- or
CC deoxyribo-nucleotide triphosphates (NTPs) (PubMed:7511411). Unwinds
CC numerous nucleic acid substrates such as double-stranded (ds) DNA and
CC RNA, DNA:RNA hybrids, DNA and RNA forks composed of either partially
CC complementary DNA duplexes or DNA:RNA hybrids, respectively, and also
CC DNA and RNA displacement loops (D- and R-loops), triplex-helical DNA
CC (H-DNA) structure and DNA and RNA-based G-quadruplexes
CC (PubMed:7511411). Binds dsDNA, single-stranded DNA (ssDNA), dsRNA,
CC ssRNA and poly(A)-containing RNA (PubMed:7511411). Binds also to
CC circular dsDNA or dsRNA of either linear and/or circular forms and
CC stimulates the relaxation of supercoiled DNAs catalyzed by
CC topoisomerase TOP2A. Plays a role in DNA replication at origins of
CC replication and cell cycle progression. Plays a role as a
CC transcriptional coactivator acting as a bridging factor between
CC polymerase II holoenzyme and transcription factors or cofactors, such
CC as BRCA1, CREBBP, RELA and SMN1. Binds to the CDKN2A promoter. Plays
CC several roles in post-transcriptional regulation of gene expression. In
CC cooperation with NUP98, promotes pre-mRNA alternative splicing
CC activities of a subset of genes. As component of a large PER complex,
CC is involved in the negative regulation of 3' transcriptional
CC termination of circadian target genes such as PER1 and NR1D1 and the
CC control of the circadian rhythms. Acts also as a nuclear resolvase that
CC is able to bind and neutralize harmful massive secondary double-
CC stranded RNA structures formed by inverted-repeat Alu retrotransposon
CC elements that are inserted and transcribed as parts of genes during the
CC process of gene transposition. Involved in the positive regulation of
CC nuclear export of constitutive transport element (CTE)-containing
CC unspliced mRNA. Component of the coding region determinant (CRD)-
CC mediated complex that promotes cytoplasmic MYC mRNA stability. Plays a
CC role in mRNA translation. Positively regulates translation of selected
CC mRNAs through its binding to post-transcriptional control element (PCE)
CC in the 5'-untranslated region (UTR). Involved with LARP6 in the
CC translation stimulation of type I collagen mRNAs for CO1A1 and CO1A2
CC through binding of a specific stem-loop structure in their 5'-UTRs.
CC Stimulates LIN28A-dependent mRNA translation probably by facilitating
CC ribonucleoprotein remodeling during the process of translation. Plays
CC also a role as a small interfering (siRNA)-loading factor involved in
CC the RNA-induced silencing complex (RISC) loading complex (RLC)
CC assembly, and hence functions in the RISC-mediated gene silencing
CC process. Binds preferentially to short double-stranded RNA, such as
CC those produced during rotavirus intestinal infection. This interaction
CC may mediate NLRP9 inflammasome activation and trigger inflammatory
CC response, including IL18 release and pyroptosis. Finally, mediates the
CC attachment of heterogeneous nuclear ribonucleoproteins (hnRNPs) to
CC actin filaments in the nucleus. {ECO:0000250|UniProtKB:Q08211}.
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:0000250|UniProtKB:Q08211};
CC -!- SUBUNIT: Component of the coding region determinant (CRD)-mediated
CC complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1.
CC Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1,
CC HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and
CC YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing
CC untranslated mRNAs. The large PER complex involved in the repression of
CC transcriptional termination is composed of at least PER2, CDK9, DDX5,
CC DHX9, NCBP1 and POLR2A (active). Associates (via DRBM domains) with the
CC RISC complex; this association occurs in a small interfering (siRNA)-
CC dependent manner. Associates with the SMN complex; this association
CC induces recruitment of DHX9 to the RNA polymerase II. Associates with
CC polysomes in a LIN28A-dependent manner. Interacts (via C-terminus) with
CC ACTB; this interaction is direct and mediates the attachment to nuclear
CC ribonucleoprotein complexes. Interacts with ADAR isoform 1; this
CC interaction occurs in a RNA-independent manner. Interacts (via DRBM
CC domains) with AGO2 (via middle region); this interaction promotes
CC active RISC assembly by promoting the association of siRNA with AGO2.
CC Interacts (via NTD domain) with AKAP8L (via N-terminus). Interacts with
CC BRCA1 (via C-terminus); this interaction is direct and links BRCA1 to
CC the RNA polymerase II holoenzyme. Interacts (via N-terminus) with
CC CREBBP; this interaction mediates association with RNA polymerase II
CC holoenzyme and stimulates CREB-dependent transcriptional activation.
CC Interacts (via N-terminus) with EIF2AK2/PKR; this interaction is
CC dependent upon the activation of the kinase. Interacts (via DRBM
CC domains) with DICER1. Interacts with H2AX; this interaction is direct,
CC requires phosphorylation of histone H2AX by PRKDC and promotes binding
CC of DHX9 to transcriptionally stalled sites on chromosomal DNA in
CC response to genotoxic stress. Interacts with HNRNPC; this interaction
CC is direct, enhanced probably by their concomitant binding to RNA and
CC mediates the attachment to actin filaments. Interacts (via NTD domain)
CC with PRMT1. Interacts with IGF2BP1. Interacts with IGF2BP2, IGF2BP3.
CC Interacts (via DRBM domains) with ILF3; this interaction occurs in a
CC RNA-independent manner. Interacts with Importin alpha/Importin beta
CC receptor. Interacts with LARP6 (via C-terminus); this interaction
CC occurs in a mRNA-independent manner. Interacts (via N- and C-terminus)
CC with LIN28A (via C-terminus); this interaction occurs in a RNA-
CC independent manner. Interacts with LMX1B. Interacts (via helicase C-
CC terminal domain, HA2 and OB-fold regions) with MAVS (via CARD domain);
CC this interaction occurs in both resting and double-stranded RNA
CC poly(I:C)-induced cells. Interacts with MBD2; this interaction
CC stimulates transcriptional activation in a CREB-dependent manner.
CC Interacts (via H2A and OB-fold regions) with MYD88 (via TIR domain);
CC this interaction is direct. Interacts with NLRP9 upon rotavirus
CC infection; this interaction may trigger NLRP9 inflammasome activation
CC and inflammatory response. Interacts (via DRBM, OB-fold and RGG
CC regions) with NUP98 (via N-terminus); this interaction occurs in a RNA-
CC dependent manner and stimulates DHX9-mediated ATPase activity and
CC regulates transcription and splicing of a subset of genes. Interacts
CC (via N-terminus) with NXF1 (via N-terminus); this interaction is direct
CC and negatively regulates NXF1-mediated nuclear export of constitutive
CC transport element (CTE)-containing cellular mRNAs. Interacts with RELA;
CC this interaction is direct and activates NF-kappa-B-mediated
CC transcription. Interacts (via MTAD region) with RNA polymerase II
CC holoenzyme; this interaction stimulates transcription activation in a
CC CREB-dependent manner. Interacts (via RGG region) with SMN1; this
CC interaction links SMN1 to the RNA polymerase II holoenzyme (ref.8).
CC Interacts with SP7. Interacts (via DRBM domains) with TARBP2 (via DRBM
CC first and second domains); this interaction occurs in a small
CC interfering (siRNA)-dependent manner. Interacts with TOP2A; this
CC interaction occurs in a E2 enzyme UBE2I- and RNA-dependent manner,
CC negatively regulates DHX9-mediated double-stranded DNA and RNA duplex
CC helicase activity and stimulates TOP2A-mediated supercoiled DNA
CC relaxation activity. Interacts (via DRBM domains and C-terminus) with
CC WRN (via 3'-5' exonuclease domain); this interaction inhibits the DNA-
CC dependent NTPase and DNA helicase activities of DHX9 and stimulates the
CC 3'-5' exonuclease activity of WRN. Interacts with XRCC5; this
CC interaction occurs in a RNA-dependent manner. Interacts with ZIC2 (via
CC C2H2-type domain 3). Interacts with MCM3AP (By similarity).
CC {ECO:0000250|UniProtKB:Q08211}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q08211}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q08211}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q08211}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q08211}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q08211}.
CC Note=Nucleoplasmic shuttling protein. Its nuclear import involves the
CC nucleocytoplasmic transport receptor Importin alpha/Importin beta
CC receptor pathway in a Ran-dependent manner. In interphase, localizes in
CC nuclear stress granules and at perichromatin fibrils and in cytoplasmic
CC ribonucleoprotein granules. Colocalizes with WRN and H2AX at
CC centrosomes in a microtubule-dependent manner following DNA damaging
CC agent treatment. Excluded from the mitotic nucleus as early as prophase
CC and re-entered the nucleus at telophase. Recruited in diffuse and
CC discrete intranuclear foci (GLFG-body) in a NUP98-dependent manner.
CC Colocalizes with SP7 in the nucleus. Colocalizes with ACTB at nuclear
CC actin filaments inside the nucleus or at the nuclear pore. Colocalizes
CC with HNRNPC at nuclear ribonucleoprotein complex proteins in the
CC nucleus. Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs. {ECO:0000250|UniProtKB:Q08211}.
CC -!- DOMAIN: DRBM domains cooperate for the binding to nucleic acid but not
CC for unwinding helicase activity. The helicase-associated domain-2 (HA2)
CC region is essential for the duplex RNA unwinding helicase activity. The
CC minimal transactivation region (MTAD) mediates interaction with the RNA
CC polymerase II holoenzyme and stimulates transcriptional activation in a
CC CREB-dependent manner. The oligonucleotide- or oligosaccharide-binding
CC (OB-fold) and the repeated arginine and glycine-glycine (RGG) regions
CC are dispensable for both RNA-binding and unwinding helicase activities.
CC The RGG region contains both nuclear localization signal (NLS) and
CC nuclear export signal (NES) and is necessary and sufficient for
CC nucleocytoplasmic shuttling in a RNA-independent manner.
CC {ECO:0000250|UniProtKB:Q08211}.
CC -!- PTM: Methylated. PRMT1-mediated methylation of undefined Arg residues
CC in the nuclear transport domain (NTD) is required for nuclear import of
CC DHX9. {ECO:0000250|UniProtKB:Q08211}.
CC -!- PTM: Phosphorylated by PRKDC; phosphorylation occurs in a RNA-dependent
CC manner. Phosphorylated by EIF2AK2/PKR; this phosphorylation reduces its
CC association with double-stranded RNA. {ECO:0000250|UniProtKB:Q08211}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {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; X82829; CAA58036.1; -; mRNA.
DR PIR; I46032; I46032.
DR RefSeq; NP_776461.1; NM_174036.2.
DR AlphaFoldDB; Q28141; -.
DR BMRB; Q28141; -.
DR SMR; Q28141; -.
DR BioGRID; 158477; 1.
DR IntAct; Q28141; 2.
DR STRING; 9913.ENSBTAP00000026409; -.
DR PaxDb; Q28141; -.
DR PeptideAtlas; Q28141; -.
DR PRIDE; Q28141; -.
DR Ensembl; ENSBTAT00000026409; ENSBTAP00000026409; ENSBTAG00000019821.
DR GeneID; 281115; -.
DR KEGG; bta:281115; -.
DR CTD; 1660; -.
DR VEuPathDB; HostDB:ENSBTAG00000019821; -.
DR VGNC; VGNC:28060; DHX9.
DR eggNOG; KOG0921; Eukaryota.
DR GeneTree; ENSGT00940000155924; -.
DR InParanoid; Q28141; -.
DR OMA; YGPETRM; -.
DR OrthoDB; 278674at2759; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000019821; Expressed in spermatocyte and 107 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR GO; GO:0097165; C:nuclear stress granule; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005726; C:perichromatin fibrils; ISS:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0016442; C:RISC complex; ISS:UniProtKB.
DR GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0033679; F:3'-5' DNA/RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003688; F:DNA replication origin binding; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0061676; F:importin-alpha family protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:UniProtKB.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; ISS:UniProtKB.
DR GO; GO:1905538; F:polysome binding; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0001069; F:regulatory region RNA binding; IEA:Ensembl.
DR GO; GO:1905172; F:RISC complex binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB.
DR GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
DR GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
DR GO; GO:1990518; F:single-stranded 3'-5' DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0035197; F:siRNA binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0045142; F:triplex DNA binding; ISS:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; ISS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IEA:Ensembl.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR GO; GO:0039695; P:DNA-templated viral transcription; IEA:Ensembl.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; ISS:UniProtKB.
DR GO; GO:0098795; P:global gene silencing by mRNA cleavage; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:Ensembl.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1905698; P:positive regulation of polysome binding; ISS:UniProtKB.
DR GO; GO:0060760; P:positive regulation of response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0050434; P:positive regulation of viral transcription; IEA:Ensembl.
DR GO; GO:1904973; P:positive regulation of viral translation; IEA:Ensembl.
DR GO; GO:1903608; P:protein localization to cytoplasmic stress granule; IEA:Ensembl.
DR GO; GO:2000765; P:regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0050684; P:regulation of mRNA processing; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0070922; P:RISC complex assembly; ISS:UniProtKB.
DR GO; GO:0010501; P:RNA secondary structure unwinding; ISS:UniProtKB.
DR CDD; cd17972; DEXHc_DHX9; 1.
DR CDD; cd19854; DSRM_DHX9_rpt1; 1.
DR CDD; cd19855; DSRM_DHX9_rpt2; 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; IPR044447; DHX9_DEXHc.
DR InterPro; IPR044445; DHX9_DSRM_1.
DR InterPro; IPR044446; DHX9_DSRM_2.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014720; dsRBD_dom.
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; PF00035; dsrm; 2.
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; SM00358; DSRM; 2.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; ATP-binding; Biological rhythms; Cytoplasm;
KW Cytoskeleton; DNA replication; DNA-binding; Helicase; Hydrolase; Immunity;
KW Inflammatory response; Innate immunity; Isopeptide bond; Manganese;
KW Metal-binding; Methylation; mRNA processing; mRNA splicing; mRNA transport;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Transcription termination;
KW Translation regulation; Transport; Ubl conjugation.
FT CHAIN 1..1287
FT /note="ATP-dependent RNA helicase A"
FT /id="PRO_0000055156"
FT DOMAIN 3..71
FT /note="DRBM 1"
FT /evidence="ECO:0000250|UniProtKB:Q08211,
FT ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 177..249
FT /note="DRBM 2"
FT /evidence="ECO:0000250|UniProtKB:Q08211,
FT ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 395..561
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08211,
FT ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 633..806
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..247
FT /note="Interaction with CREBBP"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 5..9
FT /note="siRNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 53..55
FT /note="siRNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 82..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..183
FT /note="siRNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 227..322
FT /note="Interaction with BRCA1"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 231..233
FT /note="siRNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 252..661
FT /note="Necessary for interaction with RNA polymerase II
FT holoenzyme"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 310..949
FT /note="Necessary for interaction with H2AX"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 328..377
FT /note="MTAD"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 395..806
FT /note="Core helicase"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 828..916
FT /note="HA2"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 955..1071
FT /note="OB-fold"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 1147..1276
FT /note="NTD region"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 1148..1287
FT /note="RGG"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 1253..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 508..511
FT /note="DEIH box"
FT MOTIF 583..592
FT /note="Nuclear localization signal (NLS1)"
FT /evidence="ECO:0000255"
FT MOTIF 1152..1170
FT /note="Nuclear localization signal (NLS2)"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT BINDING 408..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08211,
FT ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 415
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT BINDING 509
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 143
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O70133"
FT MOD_RES 143
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 188
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 196
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 1021
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 1163
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O70133"
FT MOD_RES 1172
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 1235
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O70133"
FT MOD_RES 1251
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O70133"
FT MOD_RES 1259
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O70133"
FT MOD_RES 1266
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O70133"
FT MOD_RES 1282
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O70133"
FT CROSSLNK 694
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
SQ SEQUENCE 1287 AA; 141944 MW; DC908095AB683ED4 CRC64;
MGDVKNFLYA WCGKRKMTPS YEIRAVGNKN RQKFMCEVRV EGYNYTGMGN STNKKDAQSN
AARDFVNYLV RINELKSEEV PAVGVAPPTP SATDSSDTTA EDGGVPGNLG GPLPPHLTLQ
AENNSGGGGS GYVPTWDRGA NLKDYYSRKE EQEVQATLES EEVDLNAGLH GNWTLENAKA
RLNQYFQKEK IQGEYKYTQV GPDHNRSFIA EMTIYIKQIG RRIFAREHGS NKKLAAQSCA
LSLVRQLYHL GVIEPYSGLT KKKEGETVEP YKVNLSQDLE HQLQNIVQEL NLEIVPIPED
PSVPVALNLG KLAQFEPSQR QNPVGVVPWS PPQSNWNPWT SSNIDEGPLA YATPEQISMD
LKNELMYQLE QDRDLQAVLQ ERELLPVKKF ESEILEAISQ NPVVIIRGAT GCGKTTQVPQ
FILDDCIQND RAAECNIVVT QPRRISAVSV AERVAYERGE EPGKSCGYSV RFESILPRPH
ASIMFCTVGV LLRKLEAGIR GISHVIVDEI HERDINTDFL LVVLRDVVQA YPEVRIVLMS
ATIDTSMFCE YFFNCPIIEV YGRTFPVQEY FLEDCIQMTH FVPPPKDKKK KDKDDDGGED
DDANCNLICG DEYGAETRIS MAQLNEKETP FELIEALLLY IETLNVPGAV LVFLPGWNLI
YTMQKHLEMN PHFGSHRYQI LPLHSQIPRE EQRKVFDPVP SGVTKIILST NIAETSITIN
DVVYVIDSCK QKVKLFTAHN NMTNYATVWA SKTNLEQRKG RAGRVRPGFC FHLCSRARFE
RLETHMTPEM FRTPLHEIAL SIKLLRLGGI GQFLAKAIEP PPLDAVIEAE HTLRELDALD
ANDELTPLGR ILAKLPIEPR FGKMMIMGCI FYVGDAICTI SAATCFPEPF ISEGKRLGYI
HRNFAGNRFS DHVALLSVFQ AWDDARMGGE EAEIRFCEHK RLNMATLRMT WEAKVQLKEI
LINSGFPEEC LLTQVFTNTG PDNNLDVVIS LLAFGVYPNV CYHKEKRKIL TTEGRNALIH
KSSVNCPFSS QDMKYPSPFF VFGEKIRTRA ISAKGMTLVT PLQLLLFASK KVQSDGQLVL
VDDWIRLQIS HEAAACITAL RAAMEALVVE VTKQPGIISQ LDPVNERMLN TIRQISRPSA
AGINLMIGTT RYGDGPRPPK MARYDNGSGY RRGGSSYSGG GYGLGGYGTG GYGGGGGYGG
RGGYSGGGYG GGSNSFRGSY VGGGGGVGGG GGGFRGLSRG GYRGMSGGDY RGESGGGYRG
SGGFQRGGGR GGYGGGYFGQ GRGGGGY
