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Q9H2U1 (DHX36_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DHX36
Synonyms:DDX36, KIAA1488, MLEL1, RHAU
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1008 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.8 Ref.10 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.18

Subunit structure

Interacts with AGO1, AGO2, PARN, EXOSC3, EXOSC10, HDAC1 and HDAC4. Ref.2 Ref.9 Ref.17 Ref.20

Subcellular location

Nucleus. Cytoplasm. Chromosometelomere Probable. 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. Ref.2 Ref.11

Tissue specificity

Highly expressed in testis. Ref.1 Ref.2

Domain

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

Sequence similarities

Belongs to the DEAD box helicase family. DEAH subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentChromosome
Cytoplasm
Nucleus
Telomere
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandATP-binding
DNA-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.18. Source: GOC

RNA secondary structure unwinding

Inferred from direct assay Ref.20. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

ossification

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of telomere maintenance

Inferred from mutant phenotype Ref.20. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

response to exogenous dsRNA

Inferred from electronic annotation. Source: Ensembl

response to virus

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromosome, telomeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

DNA-dependent ATPase activity

Inferred from direct assay Ref.18. Source: UniProtKB

G-quadruplex DNA binding

Inferred from direct assay Ref.18. Source: UniProtKB

G-quadruplex RNA binding

Inferred from mutant phenotype Ref.20. Source: UniProtKB

core promoter binding

Inferred from direct assay Ref.18. Source: UniProtKB

double-stranded RNA binding

Inferred from direct assay PubMed 21266579. Source: MGI

histone deacetylase binding

Inferred from sequence or structural similarity. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H2U1-1)

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.
Isoform 2 (identifier: Q9H2U1-2)

Also known as: Cytoplasmic isoform; RHAU-delta 14;

The sequence of this isoform differs from the canonical sequence as follows:
     517-530: Missing.
Isoform 3 (identifier: Q9H2U1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     737-765: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10081008ATP-dependent RNA helicase DHX36
PRO_0000247530

Regions

Domain217 – 387171Helicase ATP-binding
Domain477 – 647171Helicase C-terminal
Nucleotide binding230 – 2378ATP By similarity
Region1 – 105105RNA-binding; sufficient and required for recruitment to cytoplasmic stress granules
Region53 – 10553Sufficient and required for interaction with TERC 5'-end
Region54 – 6613RSM
Coiled coil72 – 15786 Potential
Motif334 – 3374DEAH box
Motif517 – 52812Nuclear localization signal
Compositional bias10 – 6354Gly-rich

Amino acid modifications

Modified residue9471N6-acetyllysine Ref.14

Natural variations

Alternative sequence517 – 53014Missing in isoform 2.
VSP_020006
Alternative sequence737 – 76529Missing in isoform 3.
VSP_020007
Natural variant1511E → K.
Corresponds to variant rs1058299 [ dbSNP | Ensembl ].
VAR_027140
Natural variant4161S → C. Ref.1 Ref.2 Ref.6
Corresponds to variant rs9438 [ dbSNP | Ensembl ].
VAR_027141
Natural variant5831I → N. Ref.6
Corresponds to variant rs17853513 [ dbSNP | Ensembl ].
VAR_027142

Experimental info

Mutagenesis541P → G: Reduces G4-RNA binding; when associated with A-57, A-59, A-62 and A-63. Ref.15
Mutagenesis571L → A: Reduces G4-RNA binding; when associated with G-54, A-59, A-62 and A-63. Ref.15
Mutagenesis591G → A: Reduces G4-RNA binding; when associated with G-54, A-57, A-62 and A-63. Ref.15
Mutagenesis591G → P: Greatly reduces G4-RNA binding; when associated with P-63. Ref.15
Mutagenesis621I → A: Reduces G4-RNA binding; when associated with G-54, A-57, A-59 and A-63. Ref.15
Mutagenesis631G → A: Reduces G4-RNA binding; when associated with G-54, A-57, A-59 and A-62. Ref.15
Mutagenesis631G → P: Greatly reduces G4-RNA binding; when associated with P-59. Ref.15
Mutagenesis3351E → A: Loss of ATPase activity resulting in loss of mRNA deadenylation and decay. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Nuclear isoform) [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: 66A28A1FE93C62AE

FASTA1,008114,760
        10         20         30         40         50         60 
MSYDYHQNWG RDGGPRSSGG GYGGGPAGGH GGNRGSGGGG GGGGGGRGGR GRHPGHLKGR 

        70         80         90        100        110        120 
EIGMWYAKKQ GQKNKEAERQ ERAVVHMDER REEQIVQLLN SVQAKNDKES EAQISWFAPE 

       130        140        150        160        170        180 
DHGYGTEVST KNTPCSENKL DIQEKKLINQ EKKMFRIRNR SYIDRDSEYL LQENEPDGTL 

       190        200        210        220        230        240 
DQKLLEDLQK KKNDLRYIEM QHFREKLPSY GMQKELVNLI DNHQVTVISG ETGCGKTTQV 

       250        260        270        280        290        300 
TQFILDNYIE RGKGSACRIV CTQPRRISAI SVAERVAAER AESCGSGNST GYQIRLQSRL 

       310        320        330        340        350        360 
PRKQGSILYC TTGIILQWLQ SDPYLSSVSH IVLDEIHERN LQSDVLMTVV KDLLNFRSDL 

       370        380        390        400        410        420 
KVILMSATLN AEKFSEYFGN CPMIHIPGFT FPVVEYLLED VIEKIRYVPE QKEHRSQFKR 

       430        440        450        460        470        480 
GFMQGHVNRQ EKEEKEAIYK ERWPDYVREL RRRYSASTVD VIEMMEDDKV DLNLIVALIR 

       490        500        510        520        530        540 
YIVLEEEDGA ILVFLPGWDN ISTLHDLLMS QVMFKSDKFL IIPLHSLMPT VNQTQVFKRT 

       550        560        570        580        590        600 
PPGVRKIVIA TNIAETSITI DDVVYVIDGG KIKETHFDTQ NNISTMSAEW VSKANAKQRK 

       610        620        630        640        650        660 
GRAGRVQPGH CYHLYNGLRA SLLDDYQLPE ILRTPLEELC LQIKILRLGG IAYFLSRLMD 

       670        680        690        700        710        720 
PPSNEAVLLS IRHLMELNAL DKQEELTPLG VHLARLPVEP HIGKMILFGA LFCCLDPVLT 

       730        740        750        760        770        780 
IAASLSFKDP FVIPLGKEKI ADARRKELAK DTRSDHLTVV NAFEGWEEAR RRGFRYEKDY 

       790        800        810        820        830        840 
CWEYFLSSNT LQMLHNMKGQ FAEHLLGAGF VSSRNPKDPE SNINSDNEKI IKAVICAGLY 

       850        860        870        880        890        900 
PKVAKIRLNL GKKRKMVKVY TKTDGLVAVH PKSVNVEQTD FHYNWLIYHL KMRTSSIYLY 

       910        920        930        940        950        960 
DCTEVSPYCL LFFGGDISIQ KDNDQETIAV DEWIVFQSPA RIAHLVKELR KELDILLQEK 

       970        980        990       1000 
IESPHPVDWN DTKSRDCAVL SAIIDLIKTQ EKATPRNFPP RFQDGYYS 

« Hide

Isoform 2 (Cytoplasmic isoform) (RHAU-delta 14) [UniParc].

Checksum: 47809C3BDA49B709
Show »

FASTA994113,153
Isoform 3 [UniParc].

Checksum: E8F39FA84E4DA91D
Show »

FASTA979111,479

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"G4 resolvase 1 tightly binds and unwinds unimolecular G4-DNA."
Giri B., Smaldino P.J., Thys R.G., Creacy S.D., Routh E.D., Hantgan R.R., Lattmann S., Nagamine Y., Akman S.A., Vaughn J.P.
Nucleic Acids Res. 39:7161-7178(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3171.1. [Q9H2U1-1]
CCDS54657.1. [Q9H2U1-2]
PIRD56236.
RefSeqNP_001107869.1. NM_001114397.1. [Q9H2U1-2]
NP_065916.2. NM_020865.2. [Q9H2U1-1]
UniGeneHs.446270.

3D structure databases

ProteinModelPortalQ9H2U1.
SMRQ9H2U1. Positions 192-911.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128022. 31 interactions.
IntActQ9H2U1. 7 interactions.
MINTMINT-3066797.
STRING9606.ENSP00000417078.

Chemistry

ChEMBLCHEMBL2040704.

PTM databases

PhosphoSiteQ9H2U1.

Polymorphism databases

DMDM313104099.

Proteomic databases

MaxQBQ9H2U1.
PaxDbQ9H2U1.
PRIDEQ9H2U1.

Protocols and materials databases

DNASU170506.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308361; ENSP00000309296; ENSG00000174953. [Q9H2U1-3]
ENST00000329463; ENSP00000330113; ENSG00000174953. [Q9H2U1-2]
ENST00000496811; ENSP00000417078; ENSG00000174953. [Q9H2U1-1]
GeneID170506.
KEGGhsa:170506.
UCSCuc003ezy.4. human. [Q9H2U1-1]
uc003ezz.4. human. [Q9H2U1-3]
uc010hvq.3. human. [Q9H2U1-2]

Organism-specific databases

CTD170506.
GeneCardsGC03M153990.
HGNCHGNC:14410. DHX36.
HPAHPA035399.
MIM612767. gene.
neXtProtNX_Q9H2U1.
PharmGKBPA27223.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1643.
HOGENOMHOG000247063.
HOVERGENHBG081438.
InParanoidQ9H2U1.
KOK14442.
OMANVEQTEF.
OrthoDBEOG7SV0TS.
PhylomeDBQ9H2U1.
TreeFamTF324744.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9H2U1.
BgeeQ9H2U1.
CleanExHS_DHX36.
GenevestigatorQ9H2U1.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR011545. 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]
PfamPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDHX36.
GenomeRNAi170506.
NextBio88959.
PROQ9H2U1.
SOURCESearch...

Entry information

Entry nameDHX36_HUMAN
AccessionPrimary (citable) accession number: Q9H2U1
Secondary accession number(s): B2RB00 expand/collapse secondary AC list , Q70JU3, Q8IYE5, Q9P240
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM