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Q08211

- DHX9_HUMAN

UniProt

Q08211 - DHX9_HUMAN

Protein

ATP-dependent RNA helicase A

Gene

DHX9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 4 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Unwinds double-stranded DNA and RNA in a 3' to 5' direction. Alteration of secondary structure may subsequently influence interactions with proteins or other nucleic acids. Functions as a transcriptional activator. Component of the CRD-mediated complex that promotes MYC mRNA stability. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms. Positively regulates HIV-1 LTR-directed gene expression.3 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi411 – 4199ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent DNA helicase activity Source: ProtInc
    3. ATP-dependent RNA helicase activity Source: ProtInc
    4. DNA binding Source: UniProtKB-KW
    5. poly(A) RNA binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. RNA helicase activity Source: ProtInc
    8. RNA polymerase II transcription factor binding Source: BHF-UCL

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cellular response to heat Source: Ensembl
    3. circadian rhythm Source: Ensembl
    4. CRD-mediated mRNA stabilization Source: UniProtKB
    5. DNA duplex unwinding Source: GOC
    6. gene expression Source: Reactome
    7. innate immune response Source: Reactome
    8. mRNA splicing, via spliceosome Source: Reactome
    9. osteoblast differentiation Source: UniProt
    10. positive regulation of type I interferon production Source: Reactome
    11. RNA splicing Source: Reactome

    Keywords - Molecular functioni

    Activator, Helicase, Hydrolase

    Keywords - Biological processi

    Biological rhythms

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent RNA helicase A (EC:3.6.4.13)
    Short name:
    RHA
    Alternative name(s):
    DEAH box protein 9
    Leukophysin
    Short name:
    LKP
    Nuclear DNA helicase II
    Short name:
    NDH II
    Gene namesi
    Name:DHX9
    Synonyms:DDX9, LKP, NDH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2750. DHX9.

    Subcellular locationi

    Nucleusnucleolus. Cytoplasm
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Can shuttle between nucleus and cytoplasm.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. CRD-mediated mRNA stability complex Source: UniProtKB
    3. cytoplasm Source: ProtInc
    4. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    5. cytosol Source: Reactome
    6. membrane Source: UniProtKB
    7. nucleolus Source: HPA
    8. nucleoplasm Source: Reactome
    9. nucleus Source: UniProtKB
    10. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi332 – 3321W → A: Abrogates transcriptional activation by the MTAD domain. 1 Publication
    Mutagenesisi339 – 3391W → A: Abrogates transcriptional activation and RNA polymerase II binding by the MTAD domain. 1 Publication
    Mutagenesisi342 – 3421W → A: Abrogates transcriptional activation by the MTAD domain. 1 Publication
    Mutagenesisi417 – 4171K → R: Abrogates transcriptional activation. 2 Publications
    Mutagenesisi1163 – 11631Missing: Abolishes nuclear localization. 1 Publication
    Mutagenesisi1166 – 11661R → L: Abolishes nuclear localization. 1 Publication
    Mutagenesisi1166 – 11661Missing: Abolishes nuclear localization. 1 Publication

    Organism-specific databases

    PharmGKBiPA27232.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12701270ATP-dependent RNA helicase APRO_0000055157Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei87 – 871Phosphoserine2 Publications
    Modified residuei146 – 1461N6-acetyllysineBy similarity
    Modified residuei191 – 1911N6-acetyllysine1 Publication
    Modified residuei199 – 1991N6-acetyllysine1 Publication
    Modified residuei321 – 3211Phosphoserine1 Publication
    Modified residuei1024 – 10241N6-acetyllysine1 Publication

    Post-translational modificationi

    Methylated. HRMT1L2 mediated methylation of undefined Arg residues in the NTD is required for nuclear localization.1 Publication
    May be phosphorylated by PRKDC/XRCC7. Phosphorylated by EIF2AK2/PKR and this phosphorylation perturbs its association with dsRNA.5 Publications

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ08211.
    PaxDbiQ08211.
    PRIDEiQ08211.

    2D gel databases

    SWISS-2DPAGEQ08211.

    PTM databases

    PhosphoSiteiQ08211.

    Miscellaneous databases

    PMAP-CutDBQ08211.

    Expressioni

    Gene expression databases

    BgeeiQ08211.
    CleanExiHS_DHX9.
    GenevestigatoriQ08211.

    Organism-specific databases

    HPAiCAB011819.
    HPA028050.
    HPA055684.

    Interactioni

    Subunit structurei

    Interacts with ZIC2, IGF2BP1, IGF2BP2, IGF2BP3, MBD2, HRMT1L2/PRMT1, RELA and LARP6. Can also interact with XRCC5 and with TOP2A in an RNA dependent manner; these interactions may be indirect. Interaction with TOP2A is promoted by UBC9. Interacts with histone H2AFX and this requires phosphorylation of H2AFX on 'Ser-139'. Interacts (via N-terminus) with EIF2AK2/PKR and this interaction is dependent upon the activation of the kinase. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. May act to directly link BRCA1, CREBBP or SMN1 and the RNA polymerase II complex. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active).14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EIF2AK2P195252EBI-352022,EBI-640775
    NXF1Q9UBU98EBI-352022,EBI-398874
    PRMT1Q998732EBI-352022,EBI-78738
    RELAQ042064EBI-352022,EBI-73886
    YBX1P6780910EBI-352022,EBI-354065
    ZMAT3Q9HA383EBI-352022,EBI-2548480

    Protein-protein interaction databases

    BioGridi108025. 195 interactions.
    DIPiDIP-31504N.
    IntActiQ08211. 54 interactions.
    MINTiMINT-5000572.
    STRINGi9606.ENSP00000356520.

    Structurei

    Secondary structure

    1
    1270
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1411
    Beta strandi20 – 289
    Beta strandi31 – 399
    Beta strandi47 – 537
    Helixi54 – 7118
    Helixi77 – 793
    Helixi170 – 1734
    Turni178 – 1803
    Helixi181 – 19111
    Beta strandi199 – 2046
    Helixi206 – 2083
    Beta strandi210 – 2189
    Helixi220 – 2223
    Beta strandi223 – 23412
    Helixi235 – 25218
    Turni341 – 3444
    Turni351 – 3544
    Helixi357 – 37418
    Helixi376 – 38611
    Helixi389 – 3935
    Helixi394 – 40310
    Beta strandi405 – 4106
    Helixi417 – 43115
    Helixi435 – 4373
    Beta strandi439 – 4468
    Helixi447 – 45913
    Turni460 – 4623
    Beta strandi467 – 4737
    Beta strandi476 – 4783
    Beta strandi482 – 4909
    Helixi491 – 50010
    Beta strandi507 – 5104
    Helixi518 – 53316
    Beta strandi537 – 5437
    Helixi549 – 5546

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LLMX-ray2.80A/B329-563[»]
    3VYXX-ray2.29A152-264[»]
    3VYYX-ray2.90A/B1-91[»]
    ProteinModelPortaliQ08211.
    SMRiQ08211. Positions 1-86, 169-263, 329-1071.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 7169DRBM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini180 – 25273DRBM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini398 – 564167Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini636 – 809174Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 250250Interaction with CREBBPAdd
    BLAST
    Regioni230 – 32596Interaction with BRCA1Add
    BLAST
    Regioni331 – 38050MTADAdd
    BLAST
    Regioni1151 – 1260110NTDAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi511 – 5144DEIH box
    Motifi586 – 59510Nuclear localization signalSequence Analysis

    Domaini

    The MTAD domain mediates interaction with the RNA polymerase II holoenzyme. The NTD domain is necessary and sufficient for nucleo-cytoplasmic shuttling and interaction with HRMT1L2 and SMN1.2 Publications

    Sequence similaritiesi

    Contains 2 DRBM (double-stranded RNA-binding) domains.PROSITE-ProRule annotation
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1643.
    HOGENOMiHOG000247063.
    HOVERGENiHBG039429.
    InParanoidiQ08211.
    KOiK13184.
    OMAiVDDWIRL.
    OrthoDBiEOG76471V.
    PhylomeDBiQ08211.
    TreeFamiTF313601.

    Family and domain databases

    Gene3Di3.30.160.20. 2 hits.
    3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR002464. DNA/RNA_helicase_DEAH_CS.
    IPR014720. dsRNA-bd_dom.
    IPR011709. DUF1605.
    IPR007502. Helicase-assoc_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00035. dsrm. 2 hits.
    PF04408. HA2. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF07717. OB_NTP_bind. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00358. DSRM. 2 hits.
    SM00847. HA2. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
    PS50137. DS_RBD. 2 hits.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    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.

    « Hide

    MGDVKNFLYA WCGKRKMTPS YEIRAVGNKN RQKFMCEVQV EGYNYTGMGN     50
    STNKKDAQSN AARDFVNYLV RINEIKSEEV PAFGVASPPP LTDTPDTTAN 100
    AEGDLPTTMG GPLPPHLALK AENNSEVGAS GYGVPGPTWD RGANLKDYYS 150
    RKEEQEVQAT LESEEVDLNA GLHGNWTLEN AKARLNQYFQ KEKIQGEYKY 200
    TQVGPDHNRS FIAEMTIYIK QLGRRIFARE HGSNKKLAAQ SCALSLVRQL 250
    YHLGVVEAYS GLTKKKEGET VEPYKVNLSQ DLEHQLQNII QELNLEILPP 300
    PEDPSVPVAL NIGKLAQFEP SQRQNQVGVV PWSPPQSNWN PWTSSNIDEG 350
    PLAFATPEQI SMDLKNELMY QLEQDHDLQA ILQERELLPV KKFESEILEA 400
    ISQNSVVIIR GATGCGKTTQ VPQFILDDFI QNDRAAECNI VVTQPRRISA 450
    VSVAERVAFE RGEEPGKSCG YSVRFESILP RPHASIMFCT VGVLLRKLEA 500
    GIRGISHVIV DEIHERDINT DFLLVVLRDV VQAYPEVRIV LMSATIDTSM 550
    FCEYFFNCPI IEVYGRTYPV QEYFLEDCIQ MTHFVPPPKD KKKKDKDDDG 600
    GEDDDANCNL ICGDEYGPET RLSMSQLNEK ETPFELIEAL LKYIETLNVP 650
    GAVLVFLPGW NLIYTMQKHL EMNPHFGSHR YQILPLHSQI PREEQRKVFD 700
    PVPVGVTKVI LSTNIAETSI TINDVVYVID SCKQKVKLFT AHNNMTNYAT 750
    VWASKTNLEQ RKGRAGRVRP GFCFHLCSRA RFERLETHMT PEMFRTPLHE 800
    IALSIKLLRL GGIGQFLAKA IEPPPLDAVI EAEHTLRELD ALDANDELTP 850
    LGRILAKLPI EPRFGKMMIM GCIFYVGDAI CTIAAATCFP EPFINEGKRL 900
    GYIHRNFAGN RFSDHVALLS VFQAWDDARM GGEEAEIRFC EHKRLNMATL 950
    RMTWEAKVQL KEILINSGFP EDCLLTQVFT NTGPDNNLDV VISLLAFGVY 1000
    PNVCYHKEKR KILTTEGRNA LIHKSSVNCP FSSQDMKYPS PFFVFGEKIR 1050
    TRAISAKGMT LVTPLQLLLF ASKKVQSDGQ IVLVDDWIKL QISHEAAACI 1100
    TGLRAAMEAL VVEVTKQPAI ISQLDPVNER MLNMIRQISR PSAAGINLMI 1150
    GSTRYGDGPR PPKMARYDNG SGYRRGGSSY SGGGYGGGYS SGGYGSGGYG 1200
    GSANSFRAGY GAGVGGGYRG VSRGGFRGNS GGDYRGPSGG YRGSGGFQRG 1250
    GGRGAYGTGY FGQGRGGGGY 1270
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201S → T in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti108 – 1092TM → HH in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti114 – 1163PPH → LHI in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti186 – 1861N → I in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti260 – 2601S → T in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti478 – 4781I → V in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti521 – 5211D → S in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti541 – 5411L → F in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti560 – 5656IIEVYG → SLKLW in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti590 – 5901D → K in AAH25245. (PubMed:16710414)Curated
    Sequence conflicti749 – 7491A → S in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti749 – 7491A → S in CAA71668. (PubMed:9111062)Curated
    Sequence conflicti768 – 7703VRP → STA in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti768 – 7703VRP → STA in CAA71668. (PubMed:9111062)Curated
    Sequence conflicti828 – 8281A → G in AAI07882. (PubMed:16710414)Curated
    Sequence conflicti899 – 8991R → Q in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti1037 – 10371K → N in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti1063 – 10631T → P in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti1063 – 10631T → P in CAA71668. (PubMed:9111062)Curated
    Sequence conflicti1140 – 11401R → E in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti1204 – 12118NSFRAGYG → TPSGRIC in AAB48855. (PubMed:8344961)Curated
    Sequence conflicti1261 – 127010FGQGRGGGGY → LDIEEEVAAIKLGYVSSVCR Q in AAB48855. (PubMed:8344961)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti894 – 8941I → V.1 Publication
    Corresponds to variant rs1049264 [ dbSNP | Ensembl ].
    VAR_052179

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 10351035Missing in isoform 2. 2 PublicationsVSP_042314Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.3. human. [Q08211-1]
    uc009wyd.3. human. [Q08211-2]

    Polymorphism databases

    DMDMi116241330.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS41444.1. [Q08211-1 ]
    RefSeqi NP_001348.2. NM_001357.4. [Q08211-1 ]
    UniGenei Hs.191518.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LLM X-ray 2.80 A/B 329-563 [» ]
    3VYX X-ray 2.29 A 152-264 [» ]
    3VYY X-ray 2.90 A/B 1-91 [» ]
    ProteinModelPortali Q08211.
    SMRi Q08211. Positions 1-86, 169-263, 329-1071.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108025. 195 interactions.
    DIPi DIP-31504N.
    IntActi Q08211. 54 interactions.
    MINTi MINT-5000572.
    STRINGi 9606.ENSP00000356520.

    PTM databases

    PhosphoSitei Q08211.

    Polymorphism databases

    DMDMi 116241330.

    2D gel databases

    SWISS-2DPAGE Q08211.

    Proteomic databases

    MaxQBi Q08211.
    PaxDbi Q08211.
    PRIDEi Q08211.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367549 ; ENSP00000356520 ; ENSG00000135829 . [Q08211-1 ]
    GeneIDi 1660.
    KEGGi hsa:1660.
    UCSCi uc001gpr.3. human. [Q08211-1 ]
    uc009wyd.3. human. [Q08211-2 ]

    Organism-specific databases

    CTDi 1660.
    GeneCardsi GC01P182808.
    H-InvDB HIX0001404.
    HIX0149309.
    HGNCi HGNC:2750. DHX9.
    HPAi CAB011819.
    HPA028050.
    HPA055684.
    MIMi 603115. gene.
    neXtProti NX_Q08211.
    PharmGKBi PA27232.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1643.
    HOGENOMi HOG000247063.
    HOVERGENi HBG039429.
    InParanoidi Q08211.
    KOi K13184.
    OMAi VDDWIRL.
    OrthoDBi EOG76471V.
    PhylomeDBi Q08211.
    TreeFami TF313601.

    Enzyme and pathway databases

    Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    GeneWikii RNA_Helicase_A.
    GenomeRNAii 1660.
    NextBioi 6832.
    PMAP-CutDB Q08211.
    PROi Q08211.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q08211.
    CleanExi HS_DHX9.
    Genevestigatori Q08211.

    Family and domain databases

    Gene3Di 3.30.160.20. 2 hits.
    3.40.50.300. 2 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR002464. DNA/RNA_helicase_DEAH_CS.
    IPR014720. dsRNA-bd_dom.
    IPR011709. DUF1605.
    IPR007502. Helicase-assoc_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00035. dsrm. 2 hits.
    PF04408. HA2. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF07717. OB_NTP_bind. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00358. DSRM. 2 hits.
    SM00847. HA2. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    PROSITEi PS00690. DEAH_ATP_HELICASE. 1 hit.
    PS50137. DS_RBD. 2 hits.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human RNA helicase A is homologous to the maleless protein of Drosophila."
      Lee C.-G., Hurwitz J.
      J. Biol. Chem. 268:16822-16830(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT VAL-894.
    2. "Leukophysin: an RNA helicase A-related molecule identified in cytotoxic T cell granules and vesicles."
      Abdelhaleem M.M., Hameed S., Klassen D., Greenberg A.H.
      J. Immunol. 156:2026-2035(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION.
    3. "Domain structure of human nuclear DNA helicase II (RNA helicase A)."
      Zhang S., Grosse F.
      J. Biol. Chem. 272:11487-11494(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain, Muscle and Uterus.
    8. "A functional interaction between the survival motor neuron complex and RNA polymerase II."
      Pellizzoni L., Charroux B., Rappsilber J., Mann M., Dreyfuss G.
      J. Cell Biol. 152:75-85(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH SMN1, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "RNA helicase A mediates association of CBP with RNA polymerase II."
      Nakajima T., Uchida C., Anderson S.F., Lee C.-G., Hurwitz J., Parvin J.D., Montminy M.
      Cell 90:1107-1112(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CREBBP AND RNA POLYMERASE II, MUTAGENESIS OF LYS-417.
    10. "BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A."
      Anderson S.F., Schlegel B.P., Nakajima T., Wolpin E.S., Parvin J.D.
      Nat. Genet. 19:254-256(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BRCA1.
    11. "The carboxyl terminus of RNA helicase A contains a bidirectional nuclear transport domain."
      Tang H., McDonald D., Middlesworth T., Hope T.J., Wong-Staal F.
      Mol. Cell. Biol. 19:3540-3550(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN NTD, MUTAGENESIS OF LYS-1163 AND ARG-1166.
    12. Cited for: DOMAIN MTAD, MUTAGENESIS OF TRP-332; TRP-339 AND TRP-342.
    13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: INTERACTION WITH MBD2.
    15. "RNA helicase A interacts with dsDNA and topoisomerase IIalpha."
      Zhou K., Choe K.-T., Zaidi Z., Wang Q., Mathews M.B., Lee C.-G.
      Nucleic Acids Res. 31:2253-2260(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TOP2A.
    16. "RNA helicase A interacts with nuclear factor kappaB p65 and functions as a transcriptional coactivator."
      Tetsuka T., Uranishi H., Sanda T., Asamitsu K., Yang J.-P., Wong-Staal F., Okamoto T.
      Eur. J. Biochem. 271:3741-3751(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RELA, MUTAGENESIS OF LYS-417.
    17. "DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent manner."
      Zhang S., Schlott B., Goerlach M., Grosse F.
      Nucleic Acids Res. 32:1-10(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH XRCC5, PHOSPHORYLATION BY PRKDC.
    18. "Arginine methylation of RNA helicase a determines its subcellular localization."
      Smith W.A., Schurter B.T., Wong-Staal F., David M.
      J. Biol. Chem. 279:22795-22798(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION.
    19. "Actinomycin D induces histone gamma-H2AX foci and complex formation of gamma-H2AX with Ku70 and nuclear DNA helicase II."
      Mischo H.E., Hemmerich P., Grosse F., Zhang S.
      J. Biol. Chem. 280:9586-9594(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH H2AFX.
    20. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "An antiviral response directed by PKR phosphorylation of the RNA helicase A."
      Sadler A.J., Latchoumanin O., Hawkes D., Mak J., Williams B.R.
      PLoS Pathog. 5:E1000311-E1000311(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EIF2AK2, PHOSPHORYLATION.
    24. "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
      Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
      RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    25. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191; LYS-199 AND LYS-1024, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "A novel role of RNA helicase A in regulation of translation of type I collagen mRNAs."
      Manojlovic Z., Stefanovic B.
      RNA 18:321-334(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN COLLAGEN MRNA STABILIZATION, INTERACTION WITH LARP6.
    29. "Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding proteins) is modulated by distinct RNA-binding domains."
      Wachter K., Kohn M., Stohr N., Huttelmaier S.
      Biol. Chem. 394:1077-1090(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3.
    30. "Crystal structure of human RNA helicase A (DHX9): structural basis for unselective nucleotide base binding in a DEAD-box variant protein."
      Schutz P., Wahlberg E., Karlberg T., Hammarstrom M., Collins R., Flores A., Schuler H.
      J. Mol. Biol. 400:768-782(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 329-563 IN COMPLEX WITH ADP, NUCLEOTIDE-BINDING, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiDHX9_HUMAN
    AccessioniPrimary (citable) accession number: Q08211
    Secondary accession number(s): B2RNV4
    , Q05CI5, Q12803, Q32Q22, Q5VY62, Q6PD69, Q99556
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 161 of the entry and version 4 of the sequence. [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

    External Data

    Dasty 3