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O70133

- DHX9_MOUSE

UniProt

O70133 - DHX9_MOUSE

Protein

ATP-dependent RNA helicase A

Gene

Dhx9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (19 Jul 2005)
      Previous versions | rss
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    Functioni

    Component of the CRD-mediated complex that promotes MYC mRNA stability. Unwinds double-stranded DNA and RNA in a 3' to 5' direction. Alterations of secondary structure may subsequently influence interactions with proteins or other nucleic acids. Functions as a transcriptional activator. 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.1 Publication

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi413 – 4208ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent helicase activity Source: InterPro
    3. DNA binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. cellular response to heat Source: MGI
    2. circadian rhythm Source: MGI

    Keywords - Molecular functioni

    Activator, Helicase, Hydrolase

    Keywords - Biological processi

    Biological rhythms

    Keywords - Ligandi

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

    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
    Short name:
    mHEL-5
    Nuclear DNA helicase II
    Short name:
    NDH II
    Gene namesi
    Name:Dhx9
    Synonyms:Ddx9
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:108177. Dhx9.

    Subcellular locationi

    Nucleusnucleolus 1 Publication. Cytoplasm By similarity
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Can shuttle between nucleus and cytoplasm By similarity.By similarity

    GO - Cellular componenti

    1. CRD-mediated mRNA stability complex Source: UniProtKB
    2. nucleolus Source: MGI
    3. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13801380ATP-dependent RNA helicase APRO_0000055158Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei148 – 1481N6-acetyllysine1 Publication
    Modified residuei193 – 1931N6-acetyllysineBy similarity
    Modified residuei201 – 2011N6-acetyllysineBy similarity
    Modified residuei323 – 3231PhosphoserineBy similarity
    Modified residuei1026 – 10261N6-acetyllysineBy similarity

    Post-translational modificationi

    Methylated.By similarity
    May be phosphorylated by PRKDC/XRCC7 By similarity. Phosphorylated by EIF2AK2/PKR and this phosphorylation perturbs its association with dsRNA.By similarity1 Publication

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiO70133.
    PaxDbiO70133.
    PRIDEiO70133.

    PTM databases

    PhosphoSiteiO70133.

    Expressioni

    Gene expression databases

    CleanExiMM_DHX9.
    GenevestigatoriO70133.

    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).3 Publications

    Protein-protein interaction databases

    BioGridi199088. 6 interactions.
    IntActiO70133. 8 interactions.
    MINTiMINT-1868227.

    Structurei

    Secondary structure

    1
    1380
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 1410
    Beta strandi20 – 278
    Beta strandi29 – 3911
    Beta strandi47 – 537
    Helixi54 – 7219
    Turni77 – 793
    Helixi172 – 1754
    Helixi180 – 19314
    Beta strandi201 – 2066
    Beta strandi212 – 22110
    Turni222 – 2254
    Beta strandi226 – 2316
    Helixi237 – 25519

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UILNMR-A163-262[»]
    1WHQNMR-A4-89[»]
    2RS6NMR-A4-89[»]
    2RS7NMR-A163-262[»]
    ProteinModelPortaliO70133.
    SMRiO70133. Positions 4-89, 168-262, 331-1073.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO70133.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 7169DRBM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini182 – 25473DRBM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini400 – 566167Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini638 – 811174Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 253253Interaction with CREBBPBy similarityAdd
    BLAST
    Regioni233 – 32896Interaction with BRCA1By similarityAdd
    BLAST
    Regioni333 – 38250MTADBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi513 – 5164DEAH box
    Motifi588 – 59710Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1171 – 1380210Arg/Gly/Ser/Tyr-richAdd
    BLAST

    Domaini

    The MTAD domain mediates interaction with the RNA polymerase II holoenzyme.By similarity

    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.
    InParanoidiO70133.
    KOiK13184.
    PhylomeDBiO70133.

    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O70133-1) [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

    MGDIKNFLYA WCGKRKMTPA YEIRAVGNKN RQKFMCEVRV EGFNYAGMGN     50
    STNKKDAQSN AARDFVNYLV RINEVKSEEV PAVGIVPPPP ILSDTSDSTA 100
    SAAEGLPAPM GGPLPPHLAL KAEENNSGVE SSGYGSPGPT WDRGANLKDY 150
    YSRKEEQEVQ ATLESEEVDL NAGLHGNWTL ENAKARLNQY FQKEKIQGEY 200
    KYTQVGPDHN RSFIAEMTIY IKQLGRRIFA REHGSNKKLA AQSCALSLVR 250
    QLYHLGVIEA YSGLTKKKEG ERVEPYKVFL SPDLELQLQN VVQELDLEIV 300
    PPPVDPSMPV ILNIGKLAHF EPSQRQNAVG VVPWSPPQSN WNPWTSSNID 350
    EGPLAYASTE QISMDLKNEL TYQMEQDHNL QSVLQERELL PVKKFEAEIL 400
    EAISSNSVVI IRGATGCGKT TQVPQYILDD FIQNDRAAEC NIVVTQPRRI 450
    SAVAVAERVA YERGEEPGKS CGYSVRFESI LPRPHASIMF CTVGVLLRKL 500
    EAGIRGISHV IVDEIHERDI NTDFLLVVLR DVVLAYPEVR IVLMSATIDT 550
    TMFCEYFFNC PIIEVYGRTF PVQEYFLEDC IQMTQFIPPP KDKKKKDKED 600
    DGGEDDDANC NLICGDEYGP ETKLSMSQLN EKETPFELIE ALLKYIETLN 650
    VPGAVLVFLP GWNLIYTMQK HLENNSHFGS HRYQILPLHS QIPREEQRKV 700
    FDPVPDGVTK VILSTNIAET SITINDVVYV IDSCKQKVKL FTAHNNMTNY 750
    ATVWASKTNL EQRKGRAGRV RPGFCFHLCS RARFDRLETH MTPEMFRTPL 800
    HEIALSIKLL RLGGIGQFLA KAIEPPPLDA IIEAEHTLRE LDALDANDEL 850
    TPLGRILAKL PIEPRFGKMM IMGCIFYVGD AVCTISAATC FPEPFISEGK 900
    RLGYIHRNFA GNRFSDHVAL LSVFQAWDDA RMSGEEAEIR FCEQKRLNMA 950
    TLRMTWEAKV QLKEILINSG FPEDCLLTQV FTNTGPDNNL DVVISLLAFG 1000
    VYPNVCYHKE KRKILTTEGR NALIHKSSVN CPFSSQDMKY PSPFFVFGEK 1050
    IRTRAISAKG MTLVTPLQLL LFASKKVQSD GQIVFIDDWI RLQISHEAAA 1100
    CITIRAAMEA LVVEVSKQPN IISQLDPVNE HMLNTIRQIS RPSAAGINLM 1150
    IGSVRYGDGP RPPKMARYDN GSGYRRGYGG GGYGGGGYGG GYGSGGFGGG 1200
    FGSGGGFGGG FNSGGGGFGS GGGGFGSGGG GFGGGGGGFS GGGGGGFGGG 1250
    RGGGGGGFGG SGGFGNGGGG YGVGGGGYGG GGGGGYGGGS GGYGGGGYGG 1300
    GEGYSISPNS YRGNYGGGGG GYRGGSQGGY RNNFGGDYRG SSGDYRGSGG 1350
    GYRGSGGFQR RGYGGGYFGQ GRGGGGGGGY 1380
    Length:1,380
    Mass (Da):149,475
    Last modified:July 19, 2005 - v2
    Checksum:i005D641CD9A4F0C9
    GO
    Isoform 2 (identifier: O70133-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         123-123: E → EA

    Note: Contains a phosphoserine at position 137.

    Show »
    Length:1,381
    Mass (Da):149,546
    Checksum:i0AB5502F91DEFB73
    GO
    Isoform 3 (identifier: O70133-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-216: Missing.

    Show »
    Length:1,164
    Mass (Da):125,615
    Checksum:iDA64E679A88D87C2
    GO

    Sequence cautioni

    The sequence AAR87796.1 differs from that shown. Reason: Intron retention.
    The sequence AAH89159.1 differs from that shown. Reason: Frameshift at positions 447 and 448.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461A → R in AAC05725. (PubMed:9480750)Curated
    Sequence conflicti136 – 1361S → A in AAC05725. (PubMed:9480750)Curated
    Sequence conflicti136 – 1361S → A in AAC05301. (PubMed:9480750)Curated
    Sequence conflicti187 – 1871L → V(PubMed:14691545)Curated
    Sequence conflicti189 – 1891Q → H in AAC05725. (PubMed:9480750)Curated
    Sequence conflicti211 – 2111R → G in BAB28848. (PubMed:16141072)Curated
    Sequence conflicti235 – 2351S → C in AAC05725. (PubMed:9480750)Curated
    Sequence conflicti257 – 2571V → C in AAC05725. (PubMed:9480750)Curated
    Sequence conflicti281 – 2811S → P in AAC05725. (PubMed:9480750)Curated
    Sequence conflicti674 – 6741N → M in AAB72087. 1 PublicationCurated
    Sequence conflicti748 – 7481T → I in AAB72087. 1 PublicationCurated
    Sequence conflicti831 – 8311I → V in AAB72087. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 216216Missing in isoform 3. 1 PublicationVSP_014778Add
    BLAST
    Alternative sequencei123 – 1231E → EA in isoform 2. 1 PublicationVSP_014779

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U91922 mRNA. Translation: AAC05725.1.
    AF023530 Genomic DNA. Translation: AAC05301.1.
    AY512925 mRNA. Translation: AAR87796.1. Sequence problems.
    BC089159 mRNA. Translation: AAH89159.1. Sequence problems.
    AK013423 mRNA. Translation: BAB28848.1.
    U92080 mRNA. Translation: AAB72087.1.
    RefSeqiNP_031868.2. NM_007842.2.
    UniGeneiMm.20000.

    Genome annotation databases

    GeneIDi13211.
    KEGGimmu:13211.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U91922 mRNA. Translation: AAC05725.1 .
    AF023530 Genomic DNA. Translation: AAC05301.1 .
    AY512925 mRNA. Translation: AAR87796.1 . Sequence problems.
    BC089159 mRNA. Translation: AAH89159.1 . Sequence problems.
    AK013423 mRNA. Translation: BAB28848.1 .
    U92080 mRNA. Translation: AAB72087.1 .
    RefSeqi NP_031868.2. NM_007842.2.
    UniGenei Mm.20000.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UIL NMR - A 163-262 [» ]
    1WHQ NMR - A 4-89 [» ]
    2RS6 NMR - A 4-89 [» ]
    2RS7 NMR - A 163-262 [» ]
    ProteinModelPortali O70133.
    SMRi O70133. Positions 4-89, 168-262, 331-1073.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199088. 6 interactions.
    IntActi O70133. 8 interactions.
    MINTi MINT-1868227.

    PTM databases

    PhosphoSitei O70133.

    Proteomic databases

    MaxQBi O70133.
    PaxDbi O70133.
    PRIDEi O70133.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 13211.
    KEGGi mmu:13211.

    Organism-specific databases

    CTDi 1660.
    MGIi MGI:108177. Dhx9.

    Phylogenomic databases

    eggNOGi COG1643.
    HOGENOMi HOG000247063.
    HOVERGENi HBG039429.
    InParanoidi O70133.
    KOi K13184.
    PhylomeDBi O70133.

    Miscellaneous databases

    ChiTaRSi DHX9. mouse.
    EvolutionaryTracei O70133.
    NextBioi 283382.
    PROi O70133.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_DHX9.
    Genevestigatori O70133.

    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. "Molecular analysis of the cDNA and genomic DNA encoding mouse RNA helicase A."
      Lee C.-G., Eki T., Okumura K., da Costa Soares V., Hurwitz J.
      Genomics 47:365-371(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-161.
      Strain: 129/Sv.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-756 (ISOFORM 3).
      Strain: C57BL/6NCr.
    3. "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] OF 1-756 (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Embryonic germ cell.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-264 (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Embryo.
    5. "mHEL-5."
      Kisielow P., Miazek A.
      Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE OF 386-919 (ISOFORMS 1/2/3).
      Strain: C57BL/6.
    6. "Nucleolar localization of murine nuclear DNA helicase II (RNA helicase A)."
      Zhang S., Herrmann C., Grosse F.
      J. Cell Sci. 112:2693-2703(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "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: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH EIF2AK2, PHOSPHORYLATION.
    10. "Feedback regulation of transcriptional termination by the mammalian circadian clock PERIOD complex."
      Padmanabhan K., Robles M.S., Westerling T., Weitz C.J.
      Science 337:599-602(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN RHYTHMS, IDENTIFICATION IN A LARGE PER COMPLEX.
    11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    12. "Solution structure of double-stranded RNA-binding motifs from hypothetical protein BAB28848."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 4-262.
    13. "Functional role of Zic2 phosphorylation in transcriptional regulation."
      Ishiguro A., Aruga J.
      FEBS Lett. 582:154-158(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZIC2.

    Entry informationi

    Entry nameiDHX9_MOUSE
    AccessioniPrimary (citable) accession number: O70133
    Secondary accession number(s): O35931
    , O54703, Q5FWY1, Q6R5F7, Q9CSA2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3