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Q9H2U1

- DHX36_HUMAN

UniProt

Q9H2U1 - DHX36_HUMAN

Protein

ATP-dependent RNA helicase DHX36

Gene

DHX36

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Proposed to have a global role in regulating mRNA expression including transcriptional regulation and mRNA stability. Binds with high affinity to and resolves tetramolecular RNA and DNA quadruplex structures. Unwinds intramolecular quadruplexes derived from the ZIC1 and the MYC promoters. Binds to quadruplex structures in the promoters of YY1 and ALPL genes and regulates their expression. Binds to telomerase RNA template component (TERC) 5'-end (nucleotides 1-43) and unwinds an internal quadruplex formation in TERC 5'-end to promote P1 helix formation; the P1 helix acts as a template boundary ensuring accurate reverse transcription and is disrupted by quadruplex formation. May be involved in regulation of telomere length. Plays a role in degradation and deadenylation of mRNAs containing in their 3'-UTR the consensus ARE sequence element. May function in sex development and spermatogenesis. May play a role in ossification.9 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi230 – 2378ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent helicase activity Source: InterPro
    3. core promoter binding Source: UniProtKB
    4. DNA-dependent ATPase activity Source: UniProtKB
    5. double-stranded RNA binding Source: MGI
    6. G-quadruplex DNA binding Source: UniProtKB
    7. G-quadruplex RNA binding Source: UniProtKB
    8. histone deacetylase binding Source: UniProtKB
    9. poly(A) RNA binding Source: UniProtKB
    10. protein binding Source: UniProtKB
    11. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. innate immune response Source: Reactome
    3. ossification Source: UniProtKB
    4. positive regulation of telomere maintenance Source: UniProtKB
    5. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    6. positive regulation of type I interferon production Source: Reactome
    7. response to exogenous dsRNA Source: Ensembl
    8. response to virus Source: Ensembl
    9. RNA secondary structure unwinding Source: UniProtKB
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_24938. TRAF6 mediated IRF7 activation.
    REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent RNA helicase DHX36 (EC:3.6.4.12, EC:3.6.4.13)
    Alternative name(s):
    DEAH box protein 36
    G4-resolvase 1
    Short name:
    G4R1
    MLE-like protein 1
    RNA helicase associated with AU-rich element ARE
    Gene namesi
    Name:DHX36
    Synonyms:DDX36, KIAA1488, MLEL1, RHAU
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:14410. DHX36.

    Subcellular locationi

    Nucleus. Cytoplasm. Chromosometelomere Curated
    Note: Isoform 1 preferentially localized to the nucleus and isoform 2 localized to the cytoplasm. However, partitioning of cellular localization between the nucleus and cytoplasm is not exclusive, as isoform 1 was also detected in the cytoplasm. Both isoforms were excluded from nucleoli. Localizes to cytoplasmic stress granules.

    GO - Cellular componenti

    1. chromosome, telomeric region Source: UniProtKB-SubCell
    2. cytosol Source: Reactome
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Nucleus, Telomere

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi54 – 541P → G: Reduces G4-RNA binding; when associated with A-57, A-59, A-62 and A-63. 1 Publication
    Mutagenesisi57 – 571L → A: Reduces G4-RNA binding; when associated with G-54, A-59, A-62 and A-63. 1 Publication
    Mutagenesisi59 – 591G → A: Reduces G4-RNA binding; when associated with G-54, A-57, A-62 and A-63. 1 Publication
    Mutagenesisi59 – 591G → P: Greatly reduces G4-RNA binding; when associated with P-63. 1 Publication
    Mutagenesisi62 – 621I → A: Reduces G4-RNA binding; when associated with G-54, A-57, A-59 and A-63. 1 Publication
    Mutagenesisi63 – 631G → A: Reduces G4-RNA binding; when associated with G-54, A-57, A-59 and A-62. 1 Publication
    Mutagenesisi63 – 631G → P: Greatly reduces G4-RNA binding; when associated with P-59. 1 Publication
    Mutagenesisi335 – 3351E → A: Loss of ATPase activity resulting in loss of mRNA deadenylation and decay. 1 Publication

    Organism-specific databases

    PharmGKBiPA27223.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10081008ATP-dependent RNA helicase DHX36PRO_0000247530Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei947 – 9471N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9H2U1.
    PaxDbiQ9H2U1.
    PRIDEiQ9H2U1.

    PTM databases

    PhosphoSiteiQ9H2U1.

    Expressioni

    Tissue specificityi

    Highly expressed in testis.2 Publications

    Gene expression databases

    ArrayExpressiQ9H2U1.
    BgeeiQ9H2U1.
    CleanExiHS_DHX36.
    GenevestigatoriQ9H2U1.

    Organism-specific databases

    HPAiHPA035399.

    Interactioni

    Subunit structurei

    Interacts with AGO1, AGO2, PARN, EXOSC3, EXOSC10, HDAC1 and HDAC4.4 Publications

    Protein-protein interaction databases

    BioGridi128022. 32 interactions.
    IntActiQ9H2U1. 7 interactions.
    MINTiMINT-3066797.
    STRINGi9606.ENSP00000417078.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H2U1.
    SMRiQ9H2U1. Positions 192-911.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini217 – 387171Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini477 – 647171Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 105105RNA-binding; sufficient and required for recruitment to cytoplasmic stress granulesAdd
    BLAST
    Regioni53 – 10553Sufficient and required for interaction with TERC 5'-endAdd
    BLAST
    Regioni54 – 6613RSMAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili72 – 15786Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi334 – 3374DEAH box
    Motifi517 – 52812Nuclear localization signalAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi10 – 6354Gly-richAdd
    BLAST

    Domaini

    The RHAU-specific motif (RSM) is required for quadruplex G4-DNA/RNA structure recognition and resolution.

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG1643.
    HOGENOMiHOG000247063.
    HOVERGENiHBG081438.
    InParanoidiQ9H2U1.
    KOiK14442.
    OMAiNVEQTEF.
    OrthoDBiEOG7SV0TS.
    PhylomeDBiQ9H2U1.
    TreeFamiTF324744.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR002464. DNA/RNA_helicase_DEAH_CS.
    IPR011709. DUF1605.
    IPR007502. Helicase-assoc_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF04408. HA2. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF07717. OB_NTP_bind. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00847. HA2. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
    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: Q9H2U1-1) [UniParc]FASTAAdd to Basket

    Also known as: Nuclear isoform

    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

    MSYDYHQNWG RDGGPRSSGG GYGGGPAGGH GGNRGSGGGG GGGGGGRGGR     50
    GRHPGHLKGR EIGMWYAKKQ GQKNKEAERQ ERAVVHMDER REEQIVQLLN 100
    SVQAKNDKES EAQISWFAPE DHGYGTEVST KNTPCSENKL DIQEKKLINQ 150
    EKKMFRIRNR SYIDRDSEYL LQENEPDGTL DQKLLEDLQK KKNDLRYIEM 200
    QHFREKLPSY GMQKELVNLI DNHQVTVISG ETGCGKTTQV TQFILDNYIE 250
    RGKGSACRIV CTQPRRISAI SVAERVAAER AESCGSGNST GYQIRLQSRL 300
    PRKQGSILYC TTGIILQWLQ SDPYLSSVSH IVLDEIHERN LQSDVLMTVV 350
    KDLLNFRSDL KVILMSATLN AEKFSEYFGN CPMIHIPGFT FPVVEYLLED 400
    VIEKIRYVPE QKEHRSQFKR GFMQGHVNRQ EKEEKEAIYK ERWPDYVREL 450
    RRRYSASTVD VIEMMEDDKV DLNLIVALIR YIVLEEEDGA ILVFLPGWDN 500
    ISTLHDLLMS QVMFKSDKFL IIPLHSLMPT VNQTQVFKRT PPGVRKIVIA 550
    TNIAETSITI DDVVYVIDGG KIKETHFDTQ NNISTMSAEW VSKANAKQRK 600
    GRAGRVQPGH CYHLYNGLRA SLLDDYQLPE ILRTPLEELC LQIKILRLGG 650
    IAYFLSRLMD PPSNEAVLLS IRHLMELNAL DKQEELTPLG VHLARLPVEP 700
    HIGKMILFGA LFCCLDPVLT IAASLSFKDP FVIPLGKEKI ADARRKELAK 750
    DTRSDHLTVV NAFEGWEEAR RRGFRYEKDY CWEYFLSSNT LQMLHNMKGQ 800
    FAEHLLGAGF VSSRNPKDPE SNINSDNEKI IKAVICAGLY PKVAKIRLNL 850
    GKKRKMVKVY TKTDGLVAVH PKSVNVEQTD FHYNWLIYHL KMRTSSIYLY 900
    DCTEVSPYCL LFFGGDISIQ KDNDQETIAV DEWIVFQSPA RIAHLVKELR 950
    KELDILLQEK IESPHPVDWN DTKSRDCAVL SAIIDLIKTQ EKATPRNFPP 1000
    RFQDGYYS 1008
    Length:1,008
    Mass (Da):114,760
    Last modified:November 30, 2010 - v2
    Checksum:i66A28A1FE93C62AE
    GO
    Isoform 2 (identifier: Q9H2U1-2) [UniParc]FASTAAdd to Basket

    Also known as: Cytoplasmic isoform, RHAU-delta 14

    The sequence of this isoform differs from the canonical sequence as follows:
         517-530: Missing.

    Show »
    Length:994
    Mass (Da):113,153
    Checksum:i47809C3BDA49B709
    GO
    Isoform 3 (identifier: Q9H2U1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         737-765: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:979
    Mass (Da):111,479
    Checksum:iE8F39FA84E4DA91D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti151 – 1511E → K.
    Corresponds to variant rs1058299 [ dbSNP | Ensembl ].
    VAR_027140
    Natural varianti416 – 4161S → C.3 Publications
    Corresponds to variant rs9438 [ dbSNP | Ensembl ].
    VAR_027141
    Natural varianti583 – 5831I → N.1 Publication
    Corresponds to variant rs17853513 [ dbSNP | Ensembl ].
    VAR_027142

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei517 – 53014Missing in isoform 2. 1 PublicationVSP_020006Add
    BLAST
    Alternative sequencei737 – 76529Missing in isoform 3. 1 PublicationVSP_020007Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF217190 mRNA. Translation: AAG36783.1.
    AJ577133 mRNA. Translation: CAE11802.1.
    AJ577134 mRNA. Translation: CAE11803.1.
    AK314435 mRNA. Translation: BAG37047.1.
    AC018452 Genomic DNA. No translation available.
    AC134026 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78761.1.
    BC036035 mRNA. Translation: AAH36035.1.
    AB040921 mRNA. Translation: BAA96012.1.
    CCDSiCCDS3171.1. [Q9H2U1-1]
    CCDS54657.1. [Q9H2U1-2]
    PIRiD56236.
    RefSeqiNP_001107869.1. NM_001114397.1. [Q9H2U1-2]
    NP_065916.2. NM_020865.2. [Q9H2U1-1]
    UniGeneiHs.446270.

    Genome annotation databases

    EnsembliENST00000308361; ENSP00000309296; ENSG00000174953. [Q9H2U1-3]
    ENST00000329463; ENSP00000330113; ENSG00000174953. [Q9H2U1-2]
    ENST00000496811; ENSP00000417078; ENSG00000174953. [Q9H2U1-1]
    GeneIDi170506.
    KEGGihsa:170506.
    UCSCiuc003ezy.4. human. [Q9H2U1-1]
    uc003ezz.4. human. [Q9H2U1-3]
    uc010hvq.3. human. [Q9H2U1-2]

    Polymorphism databases

    DMDMi313104099.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF217190 mRNA. Translation: AAG36783.1 .
    AJ577133 mRNA. Translation: CAE11802.1 .
    AJ577134 mRNA. Translation: CAE11803.1 .
    AK314435 mRNA. Translation: BAG37047.1 .
    AC018452 Genomic DNA. No translation available.
    AC134026 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78761.1 .
    BC036035 mRNA. Translation: AAH36035.1 .
    AB040921 mRNA. Translation: BAA96012.1 .
    CCDSi CCDS3171.1. [Q9H2U1-1 ]
    CCDS54657.1. [Q9H2U1-2 ]
    PIRi D56236.
    RefSeqi NP_001107869.1. NM_001114397.1. [Q9H2U1-2 ]
    NP_065916.2. NM_020865.2. [Q9H2U1-1 ]
    UniGenei Hs.446270.

    3D structure databases

    ProteinModelPortali Q9H2U1.
    SMRi Q9H2U1. Positions 192-911.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128022. 32 interactions.
    IntActi Q9H2U1. 7 interactions.
    MINTi MINT-3066797.
    STRINGi 9606.ENSP00000417078.

    Chemistry

    ChEMBLi CHEMBL2040704.

    PTM databases

    PhosphoSitei Q9H2U1.

    Polymorphism databases

    DMDMi 313104099.

    Proteomic databases

    MaxQBi Q9H2U1.
    PaxDbi Q9H2U1.
    PRIDEi Q9H2U1.

    Protocols and materials databases

    DNASUi 170506.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308361 ; ENSP00000309296 ; ENSG00000174953 . [Q9H2U1-3 ]
    ENST00000329463 ; ENSP00000330113 ; ENSG00000174953 . [Q9H2U1-2 ]
    ENST00000496811 ; ENSP00000417078 ; ENSG00000174953 . [Q9H2U1-1 ]
    GeneIDi 170506.
    KEGGi hsa:170506.
    UCSCi uc003ezy.4. human. [Q9H2U1-1 ]
    uc003ezz.4. human. [Q9H2U1-3 ]
    uc010hvq.3. human. [Q9H2U1-2 ]

    Organism-specific databases

    CTDi 170506.
    GeneCardsi GC03M153990.
    HGNCi HGNC:14410. DHX36.
    HPAi HPA035399.
    MIMi 612767. gene.
    neXtProti NX_Q9H2U1.
    PharmGKBi PA27223.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1643.
    HOGENOMi HOG000247063.
    HOVERGENi HBG081438.
    InParanoidi Q9H2U1.
    KOi K14442.
    OMAi NVEQTEF.
    OrthoDBi EOG7SV0TS.
    PhylomeDBi Q9H2U1.
    TreeFami TF324744.

    Enzyme and pathway databases

    Reactomei REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.

    Miscellaneous databases

    GeneWikii DHX36.
    GenomeRNAii 170506.
    NextBioi 88959.
    PROi Q9H2U1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H2U1.
    Bgeei Q9H2U1.
    CleanExi HS_DHX36.
    Genevestigatori Q9H2U1.

    Family and domain databases

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

    Publicationsi

    1. "Molecular cloning and characterization of human DDX36 and mouse Ddx36 genes, new members of the DEAD/H box superfamily."
      Fu J.-J., Li L.-Y., Lu G.-X.
      Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:655-661(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT CYS-416.
      Tissue: Brain.
    2. "Facilitation of mRNA deadenylation and decay by the exosome-bound, DExH protein RHAU."
      Tran H., Schilling M., Wirbelauer C., Hess D., Nagamine Y.
      Mol. Cell 13:101-111(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, INTERACTION WITH PARN; EXOSC3 AND EXOSC10, MUTAGENESIS OF GLU-335, VARIANT CYS-416.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 3), VARIANTS CYS-416 AND ASN-583.
      Tissue: Testis.
    7. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-1008 (ISOFORM 1).
      Tissue: Brain.
    8. "The DEXH protein product of the DHX36 gene is the major source of tetramolecular quadruplex G4-DNA resolving activity in HeLa cell lysates."
      Vaughn J.P., Creacy S.D., Routh E.D., Joyner-Butt C., Jenkins G.S., Pauli S., Nagamine Y., Akman S.A.
      J. Biol. Chem. 280:38117-38120(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
      Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
      EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AGO1 AND AGO2.
    10. "G4 resolvase 1 binds both DNA and RNA tetramolecular quadruplex with high affinity and is the major source of tetramolecular quadruplex G4-DNA and G4-RNA resolving activity in HeLa cell lysates."
      Creacy S.D., Routh E.D., Iwamoto F., Nagamine Y., Akman S.A., Vaughn J.P.
      J. Biol. Chem. 283:34626-34634(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BINDING TO RNA/DNA QUADRUPLEX STRUCTURES.
    11. "Recruitment of the RNA helicase RHAU to stress granules via a unique RNA-binding domain."
      Chalupnikova K., Lattmann S., Selak N., Iwamoto F., Fujiki Y., Nagamine Y.
      J. Biol. Chem. 283:35186-35198(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, RNA-BINDING.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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-947, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Role of the amino terminal RHAU-specific motif in the recognition and resolution of guanine quadruplex-RNA by the DEAH-box RNA helicase RHAU."
      Lattmann S., Giri B., Vaughn J.P., Akman S.A., Nagamine Y.
      Nucleic Acids Res. 38:6219-6233(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF PRO-54; LEU-57; GLY-59; ILE-62 AND GLY-63.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "The 5' guanosine tracts of human telomerase RNA are recognized by the G-quadruplex binding domain of the RNA helicase DHX36 and function to increase RNA accumulation."
      Sexton A.N., Collins K.
      Mol. Cell. Biol. 31:736-743(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TERC.
    18. Cited for: FUNCTION AND CATALYTIC ACTIVITY.
    19. "Yin Yang 1 contains G-quadruplex structures in its promoter and 5'-UTR and its expression is modulated by G4 resolvase 1."
      Huang W., Smaldino P.J., Zhang Q., Miller L.D., Cao P., Stadelman K., Wan M., Giri B., Lei M., Nagamine Y., Vaughn J.P., Akman S.A., Sui G.
      Nucleic Acids Res. 40:1033-1049(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "The RNA helicase RHAU (DHX36) unwinds a G4-quadruplex in human telomerase RNA and promotes the formation of the P1 helix template boundary."
      Booy E.P., Meier M., Okun N., Novakowski S.K., Xiong S., Stetefeld J., McKenna S.A.
      Nucleic Acids Res. 40:4110-4124(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TERC.

    Entry informationi

    Entry nameiDHX36_HUMAN
    AccessioniPrimary (citable) accession number: Q9H2U1
    Secondary accession number(s): B2RB00
    , Q70JU3, Q8IYE5, Q9P240
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3