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Protein

ATP-dependent RNA helicase A

Gene

DHX9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and that plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation and RNA-mediated gene silencing (PubMed:9111062, PubMed:11416126, PubMed:12711669, PubMed:15355351, PubMed:16680162, PubMed:17531811, PubMed:20669935, PubMed:21561811, PubMed:24049074, PubMed:25062910, PubMed:24990949, PubMed:28221134). Requires a 3'-single-stranded tail as entry site for acid nuclei unwinding activities as well as the binding and hydrolyzing of any of the four ribo- or deoxyribo-nucleotide triphosphates (NTPs) (PubMed:1537828). Unwinds numerous nucleic acid substrates such as double-stranded (ds) DNA and RNA, DNA:RNA hybrids, DNA and RNA forks composed of either partially complementary DNA duplexes or DNA:RNA hybrids, respectively, and also DNA and RNA displacement loops (D- and R-loops), triplex-helical DNA (H-DNA) structure and DNA and RNA-based G-quadruplexes (PubMed:20669935, PubMed:21561811, PubMed:24049074). Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing RNA (PubMed:9111062, PubMed:10198287). Binds also to circular dsDNA or dsRNA of either linear and/or circular forms and stimulates the relaxation of supercoiled DNAs catalyzed by topoisomerase TOP2A (PubMed:12711669). Plays a role in DNA replication at origins of replication and cell cycle progression (PubMed:24990949). Plays a role as a transcriptional coactivator acting as a bridging factor between polymerase II holoenzyme and transcription factors or cofactors, such as BRCA1, CREBBP, RELA and SMN1 (PubMed:11149922, PubMed:9323138, PubMed:9662397, PubMed:11038348, PubMed:11416126, PubMed:15355351, PubMed:28221134). Binds to the CDKN2A promoter (PubMed:11038348). Plays several roles in post-transcriptional regulation of gene expression (PubMed:28221134, PubMed:28355180). In cooperation with NUP98, promotes pre-mRNA alternative splicing activities of a subset of genes (PubMed:11402034, PubMed:16680162, PubMed:28221134, PubMed:28355180). As component of a large PER complex, is involved in the negative regulation of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms (By similarity). Acts also as a nuclear resolvase that is able to bind and neutralize harmful massive secondary double-stranded RNA structures formed by inverted-repeat Alu retrotransposon elements that are inserted and transcribed as parts of genes during the process of gene transposition (PubMed:28355180). Involved in the positive regulation of nuclear export of constitutive transport element (CTE)-containing unspliced mRNA (PubMed:9162007, PubMed:10924507, PubMed:11402034). Component of the coding region determinant (CRD)-mediated complex that promotes cytoplasmic MYC mRNA stability (PubMed:19029303). Plays a role in mRNA translation (PubMed:28355180). Positively regulates translation of selected mRNAs through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR) (PubMed:16680162). Involved with LARP6 in the translation stimulation of type I collagen mRNAs for CO1A1 and CO1A2 through binding of a specific stem-loop structure in their 5'-UTRs (PubMed:22190748). Stimulates LIN28A-dependent mRNA translation probably by facilitating ribonucleoprotein remodeling during the process of translation (PubMed:21247876). Plays also a role as a small interfering (siRNA)-loading factor involved in the RNA-induced silencing complex (RISC) loading complex (RLC) assembly, and hence functions in the RISC-mediated gene silencing process (PubMed:17531811). Binds preferentially to short double-stranded RNA, such as those produced during rotavirus intestinal infection (PubMed:28636595). This interaction may mediate NLRP9 inflammasome activation and trigger inflammatory response, including IL18 release and pyroptosis (PubMed:28636595). Finally, mediates the attachment of heterogeneous nuclear ribonucleoproteins (hnRNPs) to actin filaments in the nucleus (PubMed:11687588).By similarity27 Publications
(Microbial infection) Plays a role in HIV-1 replication and virion infectivity (PubMed:11096080, PubMed:19229320, PubMed:25149208, PubMed:27107641). Enhances HIV-1 transcription by facilitating the binding of RNA polymerase II holoenzyme to the proviral DNA (PubMed:11096080, PubMed:25149208). Binds (via DRBM domain 2) to the HIV-1 TAR RNA and stimulates HIV-1 transcription of transactivation response element (TAR)-containing mRNAs (PubMed:9892698, PubMed:11096080). Involved also in HIV-1 mRNA splicing and transport (PubMed:25149208). Positively regulates HIV-1 gag mRNA translation, through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR) (PubMed:16680162). Binds (via DRBM domains) to a HIV-1 double-stranded RNA region of the primer binding site (PBS)-segment of the 5'-UTR, and hence stimulates DHX9 incorporation into virions and virion infectivity (PubMed:27107641). Plays also a role as a cytosolic viral MyD88-dependent DNA and RNA sensors in plasmacytoid dendritic cells (pDCs), and hence induce antiviral innate immune responses (PubMed:20696886, PubMed:21957149). Binds (via the OB-fold region) to viral single-stranded DNA unmethylated C-phosphate-G (CpG) oligonucleotide (PubMed:20696886).8 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi418ManganeseCombined sources1 Publication1
Metal bindingi512ManganeseCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi411 – 419ATPCombined sources2 Publications9

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB
  • ATP-dependent 3'-5' DNA/RNA helicase activity Source: UniProtKB
  • ATP-dependent 3'-5' DNA helicase activity Source: UniProtKB
  • ATP-dependent 3'-5' RNA helicase activity Source: UniProtKB
  • ATP-dependent DNA helicase activity Source: UniProtKB
  • ATP-dependent RNA helicase activity Source: UniProtKB
  • chromatin DNA binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • DNA replication origin binding Source: UniProtKB
  • double-stranded DNA binding Source: UniProtKB
  • double-stranded RNA binding Source: UniProtKB
  • importin-alpha family protein binding Source: UniProtKB
  • mRNA binding Source: UniProtKB
  • nucleoside-triphosphatase activity Source: UniProtKB
  • nucleoside-triphosphate diphosphatase activity Source: UniProtKB
  • polysome binding Source: UniProtKB
  • promoter-specific chromatin binding Source: UniProtKB
  • regulatory region RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • RNA helicase activity Source: ProtInc
  • RNA polymerase binding Source: UniProtKB
  • RNA polymerase II core binding Source: UniProtKB
  • RNA polymerase II transcription coactivator activity Source: UniProtKB
  • RNA polymerase II transcription cofactor activity Source: UniProtKB
  • RNA polymerase II transcription factor binding Source: BHF-UCL
  • RNA stem-loop binding Source: UniProtKB
  • single-stranded DNA binding Source: UniProtKB
  • single-stranded DNA-dependent ATP-dependent 3'-5' DNA helicase activity Source: UniProtKB
  • single-stranded RNA binding Source: UniProtKB
  • siRNA binding Source: UniProtKB
  • triplex DNA binding Source: UniProtKB

GO - Biological processi

  • alternative mRNA splicing, via spliceosome Source: UniProtKB
  • cellular response to exogenous dsRNA Source: UniProtKB
  • cellular response to tumor necrosis factor Source: UniProtKB
  • CRD-mediated mRNA stabilization Source: UniProtKB
  • DNA duplex unwinding Source: UniProtKB
  • DNA-templated viral transcription Source: UniProtKB
  • mRNA splicing, via spliceosome Source: Reactome
  • osteoblast differentiation Source: UniProtKB
  • positive regulation of cytoplasmic translation Source: UniProtKB
  • positive regulation of DNA repair Source: UniProtKB
  • positive regulation of DNA replication Source: UniProtKB
  • positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity Source: UniProtKB
  • positive regulation of fibroblast proliferation Source: UniProtKB
  • positive regulation of interferon-alpha secretion Source: UniProtKB
  • positive regulation of interferon-beta secretion Source: UniProtKB
  • positive regulation of interleukin-6 secretion Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of response to cytokine stimulus Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of tumor necrosis factor secretion Source: UniProtKB
  • positive regulation of type I interferon production Source: Reactome
  • positive regulation of viral transcription Source: UniProtKB
  • positive regulation of viral translation Source: UniProtKB
  • protein localization to cytoplasmic stress granule Source: AgBase
  • regulation of cytoplasmic translation Source: UniProtKB
  • regulation of mRNA processing Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • rhythmic process Source: UniProtKB-KW
  • RNA processing Source: GO_Central
  • RNA secondary structure unwinding Source: UniProtKB

Keywordsi

Molecular functionActivator, DNA-binding, Helicase, Hydrolase, RNA-binding
Biological processBiological rhythms, DNA replication, Immunity, Inflammatory response, Innate immunity, mRNA processing, mRNA splicing, mRNA transport, RNA-mediated gene silencing, Transcription, Transcription regulation, Transcription termination, Translation regulation, Transport
LigandATP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.4.13. 2681.
ReactomeiR-HSA-1810476. RIP-mediated NFkB activation via ZBP1.
R-HSA-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-933542. TRAF6 mediated NF-kB activation.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase ACurated (EC:3.6.4.137 Publications)
Alternative name(s):
DEAH box protein 9
DExH-box helicase 9Imported
Leukophysin1 Publication
Short name:
LKP1 Publication
Nuclear DNA helicase II3 Publications
Short name:
NDH II2 Publications
RNA helicase A1 Publication
Gene namesi
Name:DHX9Imported
Synonyms:DDX9Imported, LKP, NDH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000135829.16.
HGNCiHGNC:2750. DHX9.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi5K → A: Reduces siRNA-binding and interaction with AGO2; when associated with A-6. 1 Publication1
Mutagenesisi6N → A: Reduces siRNA-binding; when associated with A-5. 1 Publication1
Mutagenesisi9Y → A: Inhibits siRNA-binding and interaction with AGO2. 1 Publication1
Mutagenesisi30N → A: Does not reduce siRNA-binding and interaction with AGO2. 1 Publication1
Mutagenesisi53N → A: Inhibits siRNA-binding and decreases interaction with AGO2; when associated with A-54 and A-55. 1 Publication1
Mutagenesisi54K → A: Inhibits siRNA-binding and decreases interaction with AGO2; when associated with A-53 and A-55. 1 Publication1
Mutagenesisi55K → A: Inhibits siRNA-binding and decreases interaction with AGO2; when associated with A-53 and A-54. 1 Publication1
Mutagenesisi182K → A: Reduces siRNA-binding and interaction with AGO2. 1 Publication1
Mutagenesisi186N → A: Reduces siRNA-binding and interaction with AGO2; when associated with A-187. 1 Publication1
Mutagenesisi187Q → A: Reduces siRNA-binding and interaction with AGO2; when associated with A-186. 1 Publication1
Mutagenesisi207H → A: Reduces siRNA-binding and interaction with AGO2. 1 Publication1
Mutagenesisi234N → A: Inhibits siRNA-binding and interaction with AGO2; when associated with A-235 and A-236. 1 Publication1
Mutagenesisi235K → A: Inhibits siRNA-binding and interaction with AGO2; when associated with A-234 and A-236. 1 Publication1
Mutagenesisi236K → A: Inhibits siRNA-binding and interaction with AGO2; when associated with A-234 and A-235. 1 Publication1
Mutagenesisi332W → A: Abrogates transcriptional activation by the MTAD region. No change in RNA polymerase II holoenzyme binding. 1 Publication1
Mutagenesisi339W → A: Abrogates transcriptional activation and RNA polymerase II binding by the MTAD region. No change in ATP binding and ATPase activities. 1 Publication1
Mutagenesisi342W → A: Abrogates transcriptional activation by the MTAD region. No change in RNA polymerase II holoenzyme binding. 1 Publication1
Mutagenesisi347I → A: Reduces NUP98-induced mRNA transcription and alternative splicing activities. 1 Publication1
Mutagenesisi417K → R or N: Inhibits interaction with AGO2, DICER1 and TARBP2. Abrogates helicase activity and transcriptional activation. Does not inhibit binding to origins of DNA replication. 4 Publications1
Mutagenesisi417K → R: Reduces NUP98-induced mRNA transcription and alternative splicing activities. 1 Publication1
Mutagenesisi511D → A: Does not inhibit binding to origins of DNA replication; when associated with A-512. 1 Publication1
Mutagenesisi512E → A: Does not inhibit binding to origins of DNA replication; when associated with A-511. 1 Publication1
Mutagenesisi543S → L: Does not inhibit binding to origins of DNA replication. 1 Publication1
Mutagenesisi1160R → A: Localizes in the nucleus and interacts with the importin complex. 1 Publication1
Mutagenesisi1163K → A: Localizes in the cytoplasm and does not interact with the importin complex. 1 Publication1
Mutagenesisi1163Missing : Abolishes nuclear localization. 1 Publication1
Mutagenesisi1166R → A: Localizes in the nucleus and the cytoplasm and interacts weakly with the importin complex. 1 Publication1
Mutagenesisi1166R → L: Abolishes nuclear localization. 1 Publication1
Mutagenesisi1166Missing : Abolishes nuclear localization. 1 Publication1

Organism-specific databases

DisGeNETi1660.
OpenTargetsiENSG00000135829.
PharmGKBiPA27232.

Polymorphism and mutation databases

BioMutaiDHX9.
DMDMi116241330.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000551571 – 1270ATP-dependent RNA helicase AAdd BLAST1270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei87PhosphoserineCombined sources1
Modified residuei125PhosphoserineCombined sources1
Modified residuei146N6-acetyllysine; alternateBy similarity1
Modified residuei146N6-methyllysine; alternateCombined sources1
Modified residuei191N6-acetyllysineCombined sources1
Modified residuei199N6-acetyllysineCombined sources1
Modified residuei321PhosphoserineCombined sources1
Modified residuei449PhosphoserineCombined sources1
Modified residuei506PhosphoserineCombined sources1
Cross-linki697Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1024N6-acetyllysineCombined sources1
Modified residuei1166Asymmetric dimethylarginineBy similarity1
Modified residuei1175Omega-N-methylarginineCombined sources1
Modified residuei1219Asymmetric dimethylarginineBy similarity1
Modified residuei1235Asymmetric dimethylarginineBy similarity1
Modified residuei1242Asymmetric dimethylarginineBy similarity1
Modified residuei1249Asymmetric dimethylarginineBy similarity1
Modified residuei1265Asymmetric dimethylarginineBy similarity1

Post-translational modificationi

Methylated (PubMed:15084609). PRMT1-mediated methylation of undefined Arg residues in the RGG region is required for nuclear import of DHX9 (PubMed:15084609).1 Publication
Phosphorylated by PRKDC; phosphorylation occurs in a RNA-dependent manner (PubMed:14704337). Phosphorylated by EIF2AK2/PKR; this phosphorylation reduces its association with double-stranded RNA (PubMed:19229320).2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ08211.
MaxQBiQ08211.
PaxDbiQ08211.
PeptideAtlasiQ08211.
PRIDEiQ08211.
TopDownProteomicsiQ08211-1. [Q08211-1]

2D gel databases

SWISS-2DPAGEiQ08211.

PTM databases

iPTMnetiQ08211.
PhosphoSitePlusiQ08211.
SwissPalmiQ08211.

Miscellaneous databases

PMAP-CutDBiQ08211.

Expressioni

Gene expression databases

BgeeiENSG00000135829.
CleanExiHS_DHX9.
GenevisibleiQ08211. HS.

Organism-specific databases

HPAiCAB011819.
HPA028050.
HPA055684.

Interactioni

Subunit structurei

Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1 (PubMed:19029303). Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1 (PubMed:19029303). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active) (By similarity). Associates (via DRBM domains) with the RISC complex; this association occurs in a small interfering (siRNA)-dependent manner (PubMed:17531811, PubMed:23361462). Associates with the SMN complex; this association induces recruitment of DHX9 to the RNA polymerase II (ref.8). Associates with polysomes in a LIN28A-dependent manner (PubMed:16680162, PubMed:21247876). Interacts (via C-terminus) with ACTB; this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes (PubMed:11687588). Interacts with ADAR isoform 1; this interaction occurs in a RNA-independent manner (PubMed:28355180). Interacts (via DRBM domains) with AGO2 (via middle region); this interaction promotes active RISC assembly by promoting the association of siRNA with AGO2 (PubMed:17531811, PubMed:23361462). Interacts (via RGG region) with AKAP8L (via N-terminus) (PubMed:11402034). Interacts with BRCA1 (via C-terminus); this interaction is direct and links BRCA1 to the RNA polymerase II holoenzyme (PubMed:9662397). Interacts (via N-terminus) with CREBBP; this interaction mediates association with RNA polymerase II holoenzyme and stimulates CREB-dependent transcriptional activation (PubMed:9323138). Interacts (via N-terminus) with EIF2AK2/PKR; this interaction is dependent upon the activation of the kinase (PubMed:19229320). Interacts (via DRBM domains) with DICER1 (PubMed:17531811). Interacts with H2AFX; this interaction is direct, requires phosphorylation of histone H2AFX on 'Ser-140' by PRKDC and promotes binding of DHX9 to transcriptionally stalled sites on chromosomal DNA in response to genotoxic stress (PubMed:15613478, PubMed:17498979). Interacts with HNRNPC; this interaction is direct, enhanced probably by their concomitant binding to RNA and mediates the attachment to actin filaments (PubMed:11687588). Interacts (via RGG region) with PRMT1 (PubMed:15084609). Interacts with IGF2BP1 (PubMed:17289661, PubMed:23640942). Interacts with IGF2BP2, IGF2BP3 (PubMed:23640942). Interacts (via DRBM domains) with ILF3; this interaction occurs in a RNA-independent manner (PubMed:12946349). Interacts with Importin alpha/Importin beta receptor (PubMed:16375861). Interacts with LARP6 (via C-terminus); this interaction occurs in a mRNA-independent manner (PubMed:22190748). Interacts (via N- and C-terminus) with LIN28A (via C-terminus); this interaction occurs in a RNA-independent manner (PubMed:21247876). Interacts with LMX1B (PubMed:23308148). Interacts (via helicase C-terminal domain, HA2 and OB-fold regions) with MAVS (via CARD domain); this interaction occurs in both resting and double-stranded RNA poly(I:C)-induced cells (PubMed:21957149). Interacts with MBD2; this interaction stimulates transcriptional activation in a CREB-dependent manner (PubMed:12665568). Interacts (via H2A and OB-fold regions) with MYD88 (via TIR domain); this interaction is direct (PubMed:20696886). Interacts with NLRP9 upon rotavirus infection; this interaction may trigger NLRP9 inflammasome activation and inflammatory response (PubMed:28636595). Interacts (via DRBM, OB-fold and RGG regions) with NUP98 (via N-terminus); this interaction occurs in a RNA-dependent manner and stimulates DHX9-mediated ATPase activity and regulates transcription and splicing of a subset of genes (PubMed:28221134). Interacts (via N-terminus) with NXF1 (via N-terminus); this interaction is direct and negatively regulates NXF1-mediated nuclear export of constitutive transport element (CTE)-containing cellular mRNAs (PubMed:10924507). Interacts with RELA; this interaction is direct and activates NF-kappa-B-mediated transcription (PubMed:15355351). Interacts (via MTAD region) with RNA polymerase II holoenzyme; this interaction stimulates transcription activation in a CREB-dependent manner (PubMed:11149922, PubMed:9323138, PubMed:11416126). Interacts (via RGG region) with SMN1; this interaction links SMN1 to the RNA polymerase II holoenzyme (PubMed:11149922). Interacts with SP7 (PubMed:17303075). Interacts (via DRBM domains) with TARBP2 (via DRBM first and second domains); this interaction occurs in a small interfering (siRNA)-dependent manner (PubMed:17531811, PubMed:23361462). Interacts with TOP2A; this interaction occurs in a E2 enzyme UBE2I- and RNA-dependent manner, negatively regulates DHX9-mediated double-stranded DNA and RNA duplex helicase activity and stimulates TOP2A-mediated supercoiled DNA relaxation activity (PubMed:12711669). Interacts (via DRBM domains and C-terminus) with WRN (via 3'-5' exonuclease domain); this interaction inhibits the DNA-dependent NTPase and DNA helicase activities of DHX9 and stimulates the 3'-5' exonuclease activity of WRN (PubMed:15995249). Interacts with XRCC5; this interaction occurs in a RNA-dependent manner (PubMed:14704337). Interacts with ZIC2 (via C2H2-type domain 3) (PubMed:17251188).By similarity34 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • importin-alpha family protein binding Source: UniProtKB
  • RNA polymerase binding Source: UniProtKB
  • RNA polymerase II core binding Source: UniProtKB
  • RNA polymerase II transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108025. 239 interactors.
CORUMiQ08211.
DIPiDIP-31504N.
IntActiQ08211. 94 interactors.
MINTiMINT-5000572.
STRINGi9606.ENSP00000356520.

Structurei

Secondary structure

11270
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 14Combined sources11
Beta strandi20 – 28Combined sources9
Beta strandi31 – 39Combined sources9
Beta strandi47 – 53Combined sources7
Helixi54 – 71Combined sources18
Helixi77 – 79Combined sources3
Helixi170 – 173Combined sources4
Turni178 – 180Combined sources3
Helixi181 – 191Combined sources11
Beta strandi199 – 204Combined sources6
Helixi206 – 208Combined sources3
Beta strandi210 – 218Combined sources9
Helixi220 – 222Combined sources3
Beta strandi223 – 234Combined sources12
Helixi235 – 252Combined sources18
Turni341 – 344Combined sources4
Turni351 – 354Combined sources4
Helixi357 – 374Combined sources18
Helixi376 – 386Combined sources11
Helixi389 – 393Combined sources5
Helixi394 – 403Combined sources10
Beta strandi405 – 410Combined sources6
Helixi417 – 431Combined sources15
Helixi435 – 437Combined sources3
Beta strandi439 – 446Combined sources8
Helixi447 – 459Combined sources13
Turni460 – 462Combined sources3
Beta strandi467 – 473Combined sources7
Beta strandi476 – 478Combined sources3
Beta strandi482 – 490Combined sources9
Helixi491 – 500Combined sources10
Beta strandi507 – 510Combined sources4
Helixi518 – 533Combined sources16
Beta strandi537 – 543Combined sources7
Helixi549 – 554Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LLMX-ray2.80A/B329-563[»]
3VYXX-ray2.29A169-263[»]
3VYYX-ray2.90A/B1-86[»]
ProteinModelPortaliQ08211.
SMRiQ08211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 71DRBM 1PROSITE-ProRule annotation2 PublicationsAdd BLAST69
Domaini180 – 252DRBM 2PROSITE-ProRule annotation2 PublicationsAdd BLAST73
Domaini398 – 564Helicase ATP-bindingPROSITE-ProRule annotation1 PublicationAdd BLAST167
Domaini636 – 809Helicase C-terminalPROSITE-ProRule annotationAdd BLAST174

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 250Interaction with CREBBP1 PublicationAdd BLAST250
Regioni5 – 9siRNA-bindingCombined sources1 Publication5
Regioni53 – 55siRNA-bindingCombined sources1 Publication3
Regioni182 – 186siRNA-bindingCombined sources1 Publication5
Regioni230 – 325Interaction with BRCA11 PublicationAdd BLAST96
Regioni234 – 236siRNA-binding1 Publication3
Regioni255 – 664Necessary for interaction with RNA polymerase II holoenzyme1 PublicationAdd BLAST410
Regioni313 – 952Necessary for interaction with H2AFX1 PublicationAdd BLAST640
Regioni331 – 380MTAD1 PublicationAdd BLAST50
Regioni398 – 809Core helicase1 PublicationAdd BLAST412
Regioni831 – 919HA21 PublicationAdd BLAST89
Regioni958 – 1074OB-fold3 PublicationsAdd BLAST117
Regioni1150 – 1270RGG4 PublicationsAdd BLAST121

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi511 – 514DEIH box4
Motifi586 – 595Nuclear localization signal (NLS1)Sequence analysis10
Motifi1155 – 1173Nuclear localization signal (NLS2)1 PublicationAdd BLAST19

Domaini

DRBM domains cooperate for the binding to nucleic acid but not for unwinding helicase activity (PubMed:9111062, PubMed:25062910). The helicase-associated domain-2 (HA2) region is essential for the duplex RNA unwinding helicase activity (PubMed:25062910). The minimal transactivation region (MTAD) mediates interaction with the RNA polymerase II holoenzyme and stimulates transcriptional activation in a CREB-dependent manner (PubMed:11416126). The oligonucleotide- or oligosaccharide-binding (OB-fold) and the repeated arginine and glycine-glycine (RGG) regions are dispensable for both RNA-binding and unwinding helicase activities (PubMed:25062910). The RGG region contains both nuclear localization signal (NLS) and nuclear export signal (NES) and is necessary and sufficient for nucleocytoplasmic shuttling in a RNA-independent manner (PubMed:10207077, PubMed:11149922).5 Publications

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0920. Eukaryota.
COG1643. LUCA.
GeneTreeiENSGT00760000119189.
HOGENOMiHOG000247063.
HOVERGENiHBG039429.
InParanoidiQ08211.
KOiK13184.
OMAiCSDHVAM.
OrthoDBiEOG091G0PKT.
PhylomeDBiQ08211.
TreeFamiTF313601.

Family and domain databases

InterProiView protein in InterPro
IPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR014720. dsRBD_dom.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
PfamiView protein in Pfam
PF00270. DEAD. 1 hit.
PF00035. dsrm. 2 hits.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
SMARTiView protein in SMART
SM00487. DEXDc. 1 hit.
SM00358. DSRM. 2 hits.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiView protein in PROSITE
PS00690. DEAH_ATP_HELICASE. 1 hit.
PS50137. DS_RBD. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q08211-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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        10         20         30         40         50
MGDVKNFLYA WCGKRKMTPS YEIRAVGNKN RQKFMCEVQV EGYNYTGMGN
60 70 80 90 100
STNKKDAQSN AARDFVNYLV RINEIKSEEV PAFGVASPPP LTDTPDTTAN
110 120 130 140 150
AEGDLPTTMG GPLPPHLALK AENNSEVGAS GYGVPGPTWD RGANLKDYYS
160 170 180 190 200
RKEEQEVQAT LESEEVDLNA GLHGNWTLEN AKARLNQYFQ KEKIQGEYKY
210 220 230 240 250
TQVGPDHNRS FIAEMTIYIK QLGRRIFARE HGSNKKLAAQ SCALSLVRQL
260 270 280 290 300
YHLGVVEAYS GLTKKKEGET VEPYKVNLSQ DLEHQLQNII QELNLEILPP
310 320 330 340 350
PEDPSVPVAL NIGKLAQFEP SQRQNQVGVV PWSPPQSNWN PWTSSNIDEG
360 370 380 390 400
PLAFATPEQI SMDLKNELMY QLEQDHDLQA ILQERELLPV KKFESEILEA
410 420 430 440 450
ISQNSVVIIR GATGCGKTTQ VPQFILDDFI QNDRAAECNI VVTQPRRISA
460 470 480 490 500
VSVAERVAFE RGEEPGKSCG YSVRFESILP RPHASIMFCT VGVLLRKLEA
510 520 530 540 550
GIRGISHVIV DEIHERDINT DFLLVVLRDV VQAYPEVRIV LMSATIDTSM
560 570 580 590 600
FCEYFFNCPI IEVYGRTYPV QEYFLEDCIQ MTHFVPPPKD KKKKDKDDDG
610 620 630 640 650
GEDDDANCNL ICGDEYGPET RLSMSQLNEK ETPFELIEAL LKYIETLNVP
660 670 680 690 700
GAVLVFLPGW NLIYTMQKHL EMNPHFGSHR YQILPLHSQI PREEQRKVFD
710 720 730 740 750
PVPVGVTKVI LSTNIAETSI TINDVVYVID SCKQKVKLFT AHNNMTNYAT
760 770 780 790 800
VWASKTNLEQ RKGRAGRVRP GFCFHLCSRA RFERLETHMT PEMFRTPLHE
810 820 830 840 850
IALSIKLLRL GGIGQFLAKA IEPPPLDAVI EAEHTLRELD ALDANDELTP
860 870 880 890 900
LGRILAKLPI EPRFGKMMIM GCIFYVGDAI CTIAAATCFP EPFINEGKRL
910 920 930 940 950
GYIHRNFAGN RFSDHVALLS VFQAWDDARM GGEEAEIRFC EHKRLNMATL
960 970 980 990 1000
RMTWEAKVQL KEILINSGFP EDCLLTQVFT NTGPDNNLDV VISLLAFGVY
1010 1020 1030 1040 1050
PNVCYHKEKR KILTTEGRNA LIHKSSVNCP FSSQDMKYPS PFFVFGEKIR
1060 1070 1080 1090 1100
TRAISAKGMT LVTPLQLLLF ASKKVQSDGQ IVLVDDWIKL QISHEAAACI
1110 1120 1130 1140 1150
TGLRAAMEAL VVEVTKQPAI ISQLDPVNER MLNMIRQISR PSAAGINLMI
1160 1170 1180 1190 1200
GSTRYGDGPR PPKMARYDNG SGYRRGGSSY SGGGYGGGYS SGGYGSGGYG
1210 1220 1230 1240 1250
GSANSFRAGY GAGVGGGYRG VSRGGFRGNS GGDYRGPSGG YRGSGGFQRG
1260 1270
GGRGAYGTGY FGQGRGGGGY
Length:1,270
Mass (Da):140,958
Last modified:October 17, 2006 - v4
Checksum:iA607DA8F4C4B217A
GO
Isoform 2 (identifier: Q08211-2) [UniParc]FASTAAdd to basket
Also known as: Leukophysin, LKP

The sequence of this isoform differs from the canonical sequence as follows:
     1-1035: Missing.

Show »
Length:235
Mass (Da):24,336
Checksum:iB8A0D4E0C604A090
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti20S → T in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti108 – 109TM → HH in AAB48855 (PubMed:8344961).Curated2
Sequence conflicti114 – 116PPH → LHI in AAB48855 (PubMed:8344961).Curated3
Sequence conflicti186N → I in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti260S → T in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti478I → V in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti521D → S in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti541L → F in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti560 – 565IIEVYG → SLKLW in AAB48855 (PubMed:8344961).Curated6
Sequence conflicti590D → K in AAH25245 (PubMed:16710414).Curated1
Sequence conflicti749A → S in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti749A → S in CAA71668 (PubMed:9111062).Curated1
Sequence conflicti768 – 770VRP → STA in AAB48855 (PubMed:8344961).Curated3
Sequence conflicti768 – 770VRP → STA in CAA71668 (PubMed:9111062).Curated3
Sequence conflicti828A → G in AAI07882 (PubMed:16710414).Curated1
Sequence conflicti899R → Q in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti1037K → N in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti1063T → P in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti1063T → P in CAA71668 (PubMed:9111062).Curated1
Sequence conflicti1140R → E in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti1204 – 1211NSFRAGYG → TPSGRIC in AAB48855 (PubMed:8344961).Curated8
Sequence conflicti1261 – 1270FGQGRGGGGY → LDIEEEVAAIKLGYVSSVCR Q in AAB48855 (PubMed:8344961).Curated10

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052179894I → V1 PublicationCorresponds to variant dbSNP:rs1049264Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0423141 – 1035Missing in isoform 2. 2 PublicationsAdd BLAST1035

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13848 mRNA. Translation: AAB48855.1.
U03643 mRNA. Translation: AAA03571.1.
Y10658 mRNA. Translation: CAA71668.1.
AB451248 mRNA. Translation: BAG70062.1.
AB451372 mRNA. Translation: BAG70186.1.
AL355999, AL662837 Genomic DNA. Translation: CAH71701.1.
AL662837, AL355999 Genomic DNA. Translation: CAI19277.1.
CH471067 Genomic DNA. Translation: EAW91138.1.
BC025245 mRNA. Translation: AAH25245.1.
BC058896 mRNA. Translation: AAH58896.1.
BC107881 mRNA. Translation: AAI07882.1.
BC137136 mRNA. Translation: AAI37137.1.
CCDSiCCDS41444.1. [Q08211-1]
RefSeqiNP_001348.2. NM_001357.4. [Q08211-1]
UniGeneiHs.191518.

Genome annotation databases

EnsembliENST00000367549; ENSP00000356520; ENSG00000135829. [Q08211-1]
GeneIDi1660.
KEGGihsa:1660.
UCSCiuc001gpr.4. human. [Q08211-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiDHX9_HUMAN
AccessioniPrimary (citable) accession number: Q08211
Secondary accession number(s): B2RNV4
, Q05CI5, Q12803, Q32Q22, Q5VY62, Q6PD69, Q99556
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 17, 2006
Last modified: September 27, 2017
This is version 195 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families