DHX9_PONAB
ID DHX9_PONAB Reviewed; 1269 AA.
AC Q5R874;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
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};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Requires a 3'-single-stranded tail as
CC entry site for acid nuclei unwinding activities as well as the binding
CC and hydrolyzing of any of the four ribo- or deoxyribo-nucleotide
CC triphosphates (NTPs). Unwinds numerous nucleic acid substrates such as
CC double-stranded (ds) DNA and RNA, DNA:RNA hybrids, DNA and RNA forks
CC composed of either partially complementary DNA duplexes or DNA:RNA
CC hybrids, respectively, and also DNA and RNA displacement loops (D- and
CC R-loops), triplex-helical DNA (H-DNA) structure and DNA and RNA-based
CC G-quadruplexes. Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA
CC and poly(A)-containing RNA. Binds also to circular dsDNA or dsRNA of
CC either linear and/or circular forms and stimulates the relaxation of
CC supercoiled DNAs catalyzed by topoisomerase TOP2A. Plays a role in DNA
CC replication at origins of replication and cell cycle progression. Plays
CC a role as a transcriptional coactivator acting as a bridging factor
CC between polymerase II holoenzyme and transcription factors or
CC cofactors, such as BRCA1, CREBBP, RELA and SMN1. Binds to the CDKN2A
CC promoter. Plays several roles in post-transcriptional regulation of
CC gene expression. In cooperation with NUP98, promotes pre-mRNA
CC alternative splicing activities of a subset of genes. As component of a
CC large PER complex, is involved in the negative regulation of 3'
CC transcriptional termination of circadian target genes such as PER1 and
CC NR1D1 and the control of the circadian rhythms. Acts also as a nuclear
CC resolvase that is able to bind and neutralize harmful massive secondary
CC double-stranded RNA structures formed by inverted-repeat Alu
CC retrotransposon elements that are inserted and transcribed as parts of
CC genes during the process of gene transposition. Involved in the
CC positive regulation of nuclear export of constitutive transport element
CC (CTE)-containing unspliced mRNA. Component of the coding region
CC determinant (CRD)-mediated complex that promotes cytoplasmic MYC mRNA
CC stability. Plays a role in mRNA translation. Positively regulates
CC translation of selected mRNAs through its binding to post-
CC transcriptional control element (PCE) in the 5'-untranslated region
CC (UTR). Involved with LARP6 in the translation stimulation of type I
CC collagen mRNAs for CO1A1 and CO1A2 through binding of a specific stem-
CC loop structure in their 5'-UTRs. Stimulates LIN28A-dependent mRNA
CC translation probably by facilitating ribonucleoprotein remodeling
CC during the process of translation. Also plays a role as a small
CC interfering (siRNA)-loading factor involved in the RNA-induced
CC silencing complex (RISC) loading complex (RLC) assembly, and hence
CC functions in the RISC-mediated gene silencing process. Binds
CC preferentially to short double-stranded RNA, such as those produced
CC during rotavirus intestinal infection. This interaction may mediate
CC NLRP9 inflammasome activation and trigger inflammatory response,
CC including IL18 release and pyroptosis. Finally, mediates the attachment
CC of heterogeneous nuclear ribonucleoproteins (hnRNPs) to actin filaments
CC 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 (By similarity). The large PER complex involved in
CC the repression of transcriptional termination is composed of at least
CC PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active) (By similarity).
CC Associates (via DRBM domains) with the RISC complex; this association
CC occurs in a small interfering (siRNA)-dependent manner. Associates with
CC the SMN complex; this association induces recruitment of DHX9 to the
CC RNA polymerase II. Associates with polysomes in a LIN28A-dependent
CC manner. Interacts (via C-terminus) with ACTB; this interaction is
CC direct and mediates the attachment to nuclear ribonucleoprotein
CC complexes. Interacts with ADAR isoform 1; this interaction occurs in a
CC RNA-independent manner. Interacts (via DRBM domains) with AGO2 (via
CC middle region); this interaction promotes active RISC assembly by
CC promoting the association of siRNA with AGO2. Interacts (via NTD
CC domain) with AKAP8L (via N-terminus). Interacts with BRCA1 (via C-
CC terminus); this interaction is direct and links BRCA1 to the RNA
CC polymerase II holoenzyme. Interacts (via N-terminus) with CREBBP; this
CC interaction mediates association with RNA polymerase II holoenzyme and
CC stimulates CREB-dependent transcriptional activation. Interacts (via N-
CC terminus) with EIF2AK2/PKR; this interaction is dependent upon the
CC activation of the kinase. Interacts (via DRBM domains) with DICER1.
CC Interacts with H2AX; this interaction is direct, requires
CC phosphorylation of histone H2AX by PRKDC and promotes binding of DHX9
CC to transcriptionally stalled sites on chromosomal DNA in response to
CC genotoxic stress. Interacts with HNRNPC; this interaction is direct,
CC enhanced probably by their concomitant binding to RNA and mediates the
CC attachment to actin filaments. Interacts (via NTD domain) with PRMT1.
CC Interacts with IGF2BP1. Interacts with IGF2BP2, IGF2BP3. Interacts (via
CC DRBM domains) with ILF3; this interaction occurs in a RNA-independent
CC manner. Interacts with Importin alpha/Importin beta receptor. Interacts
CC with LARP6 (via C-terminus); this interaction occurs in a mRNA-
CC independent manner. Interacts (via N- and C-terminus) with LIN28A (via
CC C-terminus); this interaction occurs in a RNA-independent manner.
CC Interacts with LMX1B. Interacts (via helicase C-terminal domain, HA2
CC and OB-fold regions) with MAVS (via CARD domain); this interaction
CC occurs in both resting and double-stranded RNA poly(I:C)-induced cells.
CC Interacts with MBD2; this interaction stimulates transcriptional
CC activation in a CREB-dependent manner. Interacts (via H2A and OB-fold
CC regions) with MYD88 (via TIR domain); this interaction is direct.
CC Interacts with NLRP9 upon rotavirus infection; this interaction may
CC trigger NLRP9 inflammasome activation and inflammatory response.
CC Interacts (via DRBM, OB-fold and RGG regions) with NUP98 (via N-
CC terminus); this interaction occurs in a RNA-dependent manner and
CC stimulates DHX9-mediated ATPase activity and regulates transcription
CC and splicing of a subset of genes. Interacts (via N-terminus) with NXF1
CC (via N-terminus); this interaction is direct and negatively regulates
CC NXF1-mediated nuclear export of constitutive transport element (CTE)-
CC containing cellular mRNAs. Interacts with RELA; this interaction is
CC direct and activates NF-kappa-B-mediated transcription. Interacts (via
CC MTAD region) with RNA polymerase II holoenzyme; this interaction
CC stimulates transcription activation in a CREB-dependent manner.
CC Interacts (via RGG region) with SMN1; this interaction links SMN1 to
CC the RNA polymerase II holoenzyme (ref.8). Interacts with SP7. Interacts
CC (via DRBM domains) with TARBP2 (via DRBM first and second domains);
CC this interaction occurs in a small interfering (siRNA)-dependent
CC manner. Interacts with TOP2A; this interaction occurs in a E2 enzyme
CC UBE2I- and RNA-dependent manner, negatively regulates DHX9-mediated
CC double-stranded DNA and RNA duplex helicase activity and stimulates
CC TOP2A-mediated supercoiled DNA relaxation activity. Interacts (via DRBM
CC domains and C-terminus) with WRN (via 3'-5' exonuclease domain); this
CC interaction inhibits the DNA-dependent NTPase and DNA helicase
CC activities of DHX9 and stimulates the 3'-5' exonuclease activity of
CC WRN. Interacts with XRCC5; this interaction occurs in a RNA-dependent
CC manner. Interacts with ZIC2 (via C2H2-type domain 3) (By similarity).
CC Interacts with MCM3AP (By similarity). {ECO:0000250|UniProtKB:O70133,
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}.
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DR EMBL; CR859880; CAH92036.1; -; mRNA.
DR RefSeq; XP_002809755.1; XM_002809709.3.
DR RefSeq; XP_009238528.1; XM_009240253.1.
DR AlphaFoldDB; Q5R874; -.
DR BMRB; Q5R874; -.
DR SMR; Q5R874; -.
DR STRING; 9601.ENSPPYP00000000490; -.
DR Ensembl; ENSPPYT00000000510; ENSPPYP00000000490; ENSPPYG00000000431.
DR GeneID; 100449914; -.
DR KEGG; pon:100449914; -.
DR CTD; 1660; -.
DR eggNOG; KOG0921; Eukaryota.
DR GeneTree; ENSGT00940000155924; -.
DR HOGENOM; CLU_001832_1_2_1; -.
DR InParanoid; Q5R874; -.
DR OrthoDB; 278674at2759; -.
DR TreeFam; TF313601; -.
DR Proteomes; UP000001595; Chromosome 1.
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; IEA:UniProtKB-SubCell.
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; ISS: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; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; ISS: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; ISS: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; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; ISS: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; ISS: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 2: Evidence at transcript 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..1269
FT /note="ATP-dependent RNA helicase A"
FT /id="PRO_0000055159"
FT DOMAIN 3..71
FT /note="DRBM 1"
FT /evidence="ECO:0000250|UniProtKB:Q08211,
FT ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 180..252
FT /note="DRBM 2"
FT /evidence="ECO:0000250|UniProtKB:Q08211,
FT ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 398..564
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08211,
FT ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 636..809
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..250
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 83..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..186
FT /note="siRNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 230..325
FT /note="Interaction with BRCA1"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 234..236
FT /note="siRNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 255..664
FT /note="Necessary for interaction with RNA polymerase II
FT holoenzyme"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 313..952
FT /note="Necessary for interaction with H2AX"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 331..380
FT /note="MTAD"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 398..809
FT /note="Core helicase"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 588..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..919
FT /note="HA2"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 958..1074
FT /note="OB-fold"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 1150..1258
FT /note="NTD region"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 1151..1269
FT /note="RGG"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 1228..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 511..514
FT /note="DEIH box"
FT MOTIF 586..595
FT /note="Nuclear localization signal (NLS1)"
FT /evidence="ECO:0000255"
FT MOTIF 1155..1173
FT /note="Nuclear localization signal (NLS2)"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT BINDING 411..419
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08211,
FT ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 418
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT BINDING 512
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 146
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O70133"
FT MOD_RES 146
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 191
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 1024
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 1166
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O70133"
FT MOD_RES 1175
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 1218
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O70133"
FT MOD_RES 1234
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O70133"
FT MOD_RES 1241
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O70133"
FT MOD_RES 1248
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O70133"
FT MOD_RES 1264
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O70133"
FT CROSSLNK 697
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
SQ SEQUENCE 1269 AA; 140917 MW; 7C69F2F3248C9187 CRC64;
MGDVKNFLYA WCGKRKMTPS YEIRAVGNKN RQKFMCEVQV EGYNYTGMGN STNKKDAQSN
AARDFVNYLV RINEIKSEEV PAFGVASPPP LTDTPDTTAN AEGDLPTTMG GPLPPHLALK
AENNSEVGAS GYGVPGPTWD RGANLKDYYS RKEEQEVQAT LESEEVDLNA GLHGNWTLEN
AKARLNQYFQ KEKIQGEYKY TQVGPDHNRS FIAEMTIYIK QLGRRIFARE HGSNKKLAAQ
SCALSLVRQL YHLGVVEAYS GLTKKKEGET VEPYKVNLSQ DLEHQLQNII QELNLEILPP
PEDPSVPVAL NIGKLAQFEP SQRQNQVGVV PWSPPQSNWN PWTSSNIDEG PLAFATPEQI
SMDLKNELMY QLEQDHDLQA ILQERELLPV KKFESEILEA ISQNSVVIIR GATGCGKTTQ
VPQFILDDFI QNDRAAECNI VVTQPRRISA VSVAERVAFE RGEEPGKSCG YSVRFESILP
RPHASIMFCT VGVLLRKLEA GIRGISHVIV DEIHERDINT DFLLVVLRDV VQAYPEVRIV
LMSATIDTSM FCEYFFNCPI IEVYGRTYPV QEYFLEDCIQ MTHFVPPPKD KKKKDKDDDG
GEDDDANCNL ICGDEYGPET RLSMSQLNEK ETPFELIEAL LKYIETLNVP GAVLVFLPGW
NLIYTMQKHL EMNPHFGSHR YQILPLHSQI PREEQRKVFD PVPVGVTKVI LSTNIAETSI
TINDVVYVID SCKQKVKLFT AHNNMTNYAT VWASKTNLEQ RKGRAGRVRP GFCFHLCSRA
RFERLETHMT PEMFRTPLHE IALSIKLLRL GGIGQFLAKA IEPPPLDAVI EAEHTLRELD
ALDANDELTP LGRILAKLPI EPRFGKMMIM GCIFYVGDAI CTIAAATCFP EPFINEGKRL
GYIHRNFAGN RFSDHVALLS VFQAWDDARM GGEEAEIRFC EHKRLNMATL RMTWEAKVQL
KEILINSGFP EDCLLTQVFT NTGPDNNLDV VISLLAFGVY PNVCYHKEKR KILTTEGRNA
LIHKSSVNCP FSSQDMKYPS PFFVFGEKIR TRAISAKGMT LVTPLQLLLF ASKKVQSDGQ
IVLVDDWIKL QISHEAAACI TGLRAAMEAL VVEVTKQPAI ISQLDPVNER MLNMIRQISR
PSAAGINLMI GSTRYGDGPR PPKMARYDNG SGYRRGGSSY SGGGYGSGYS SGGYGSGGYG
GSANSFRAGY GGVGGGYRGV SRGGFRGNSG GDYRGPSGGY RGSGGFQRGG GRGAYGTGYF
GQGRGGGGY
