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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}.
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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
 
 
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