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Protein

ATP-dependent RNA helicase DHX36

Gene

Dhx36

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi223 – 2308ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • ossification Source: UniProtKB
  • positive regulation of telomere maintenance Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • response to exogenous dsRNA Source: MGI
  • response to virus Source: MGI
  • RNA secondary structure unwinding Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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

ReactomeiR-MMU-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-MMU-933541. TRAF6 mediated IRF7 activation.
R-MMU-975110. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DHX36 (EC:3.6.4.13)
Alternative name(s):
DEAH box protein 36
MLE-like protein 1
RNA helicase associated with AU-rich element ARE
Gene namesi
Name:Dhx36
Synonyms:Ddx36, Kiaa1488, Mlel1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1919412. Dhx36.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus, Telomere

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10011001ATP-dependent RNA helicase DHX36PRO_0000247531Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei940 – 9401N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8VHK9.
MaxQBiQ8VHK9.
PaxDbiQ8VHK9.
PRIDEiQ8VHK9.

PTM databases

iPTMnetiQ8VHK9.
PhosphoSiteiQ8VHK9.

Expressioni

Gene expression databases

CleanExiMM_DHX36.
GenevisibleiQ8VHK9. MM.

Interactioni

Subunit structurei

Interacts with AGO1, AGO2, PARN, EXOSC3, EXOSC10, HDAC1 and HDAC4.1 Publication

GO - Molecular functioni

  • histone deacetylase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi215193. 3 interactions.
DIPiDIP-48576N.
IntActiQ8VHK9. 2 interactions.
STRINGi10090.ENSMUSP00000029336.

Structurei

3D structure databases

ProteinModelPortaliQ8VHK9.
SMRiQ8VHK9. Positions 188-904.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini210 – 380171Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini470 – 640171Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9898RNA-binding; sufficient and required for recruitment to cytoplasmic stress granulesBy similarityAdd
BLAST
Regioni46 – 9853Sufficient and required for interaction with TERC 5'-endBy similarityAdd
BLAST
Regioni47 – 5913RSMAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili120 – 14728Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi327 – 3304DEAH box
Motifi510 – 52112Nuclear localization signalBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 4432Gly-richAdd
BLAST

Domaini

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

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

eggNOGiKOG0920. Eukaryota.
COG1643. LUCA.
GeneTreeiENSGT00760000119189.
HOGENOMiHOG000247063.
HOVERGENiHBG081438.
InParanoidiQ8VHK9.
KOiK14442.
OMAiKRTFRIR.
OrthoDBiEOG7SV0TS.
TreeFamiTF324744.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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]

Sequencei

Sequence statusi: Complete.

Q8VHK9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYDYHQSWS RDGGPRGSGQ GSSGGGGGGS RGSGGGGGGR GGRGRHPAHL
60 70 80 90 100
KGREIGLWYA KKQTQKNKEA ERQERAVVHM DERREEQIVQ LLNSVQAKTD
110 120 130 140 150
KDSEAQISWF APEDHGYGTE VSSEKKINSE KKLDNQEKKL LNQEKKTFRI
160 170 180 190 200
TDKSYIDRDS EYLLQENEPN LSLDQHLLED LQRKKTDPRY IEMQRFRKKL
210 220 230 240 250
PSYGMQKELV NLINNHQVTV ISGETGCGKT TQVTQFILDN YIERGKGSAC
260 270 280 290 300
RIVCTQPRRI SAISVAERVA TERAESCGNG NSTGYQIRLQ SRLPRKQGSI
310 320 330 340 350
LYCTTGIILQ WLQSDSRLSS VSHIVLDEIH ERNLQSDVLM TVIKDLLHFR
360 370 380 390 400
SDLKVILMSA TLNAEKFSEY FGNCPMIHIP GFTFPVVEYL LEDIIEKIRY
410 420 430 440 450
VPDQKEHRSQ FKRGFMQGHV NRQEKEEKEA IYKERWPAYI KELRTRYSAS
460 470 480 490 500
TVDVLQMMDD DKVDLNLIAA LIRYIVLEEE DGAILVFLPG WDNISTLHDL
510 520 530 540 550
LMSQVMFKSD KFLIIPLHSL MPTVNQTQVF KKTPPGVRKI VIATNIAETS
560 570 580 590 600
ITIDDVVYVI DGGKIKETHF DTQNNISTMS AEWVSKANAK QRKGRAGRVQ
610 620 630 640 650
PGHCYHLYNG LRASLLDDYQ LPEILRTPLE ELCLQIKILR LGGIAYFLSR
660 670 680 690 700
LMDPPSNEAV VLSIKHLMEL SALDKQEELT PLGVHLARLP VEPHIGKMIL
710 720 730 740 750
FGALFCCLDP VLTIAASLSF KDPFVIPLGK EKIADARRKE LAKETRSDHL
760 770 780 790 800
TVVNAFEGWE EAKRRGFRYE KDYCWEYFLS SNTLQMLHNM KGQFAEHLLG
810 820 830 840 850
AGFVSSRSPK DPKANINSDN EKIIKAVICA GLYPKVAKIR LNLGKKRKMV
860 870 880 890 900
KVHTKSDGLV SIHPKSVNVE QTDFHYNWLI YHLKMRTSSI YLYDCTEVSP
910 920 930 940 950
YCLLFFGGDI SIQKDKDQEI IAVDEWIVFQ SPERIAHLVK GLRKELDSLL
960 970 980 990 1000
QEKIESPHPV DWDDTKSRDC AVLSAILDLI KTQEKATPRN LPPRSQDGYY

S
Length:1,001
Mass (Da):113,883
Last modified:October 3, 2012 - v2
Checksum:i4DD9292011B8155A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291Missing in BAC98183 (PubMed:14621295).Curated
Sequence conflicti160 – 1601S → T in BAC98183 (PubMed:14621295).Curated
Sequence conflicti984 – 9841E → K in AAL47006 (PubMed:12198572).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF448804 mRNA. Translation: AAL47006.1.
AC114424 Genomic DNA. No translation available.
CH466530 Genomic DNA. Translation: EDL35384.1.
AK129373 mRNA. Translation: BAC98183.1.
AK013031 mRNA. Translation: BAB28610.1.
CCDSiCCDS17379.1.
RefSeqiNP_082412.2. NM_028136.2.
XP_011238540.1. XM_011240238.1.
XP_011238541.1. XM_011240239.1.
UniGeneiMm.224233.

Genome annotation databases

EnsembliENSMUST00000029336; ENSMUSP00000029336; ENSMUSG00000027770.
GeneIDi72162.
KEGGimmu:72162.
UCSCiuc008pjn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF448804 mRNA. Translation: AAL47006.1.
AC114424 Genomic DNA. No translation available.
CH466530 Genomic DNA. Translation: EDL35384.1.
AK129373 mRNA. Translation: BAC98183.1.
AK013031 mRNA. Translation: BAB28610.1.
CCDSiCCDS17379.1.
RefSeqiNP_082412.2. NM_028136.2.
XP_011238540.1. XM_011240238.1.
XP_011238541.1. XM_011240239.1.
UniGeneiMm.224233.

3D structure databases

ProteinModelPortaliQ8VHK9.
SMRiQ8VHK9. Positions 188-904.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215193. 3 interactions.
DIPiDIP-48576N.
IntActiQ8VHK9. 2 interactions.
STRINGi10090.ENSMUSP00000029336.

PTM databases

iPTMnetiQ8VHK9.
PhosphoSiteiQ8VHK9.

Proteomic databases

EPDiQ8VHK9.
MaxQBiQ8VHK9.
PaxDbiQ8VHK9.
PRIDEiQ8VHK9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029336; ENSMUSP00000029336; ENSMUSG00000027770.
GeneIDi72162.
KEGGimmu:72162.
UCSCiuc008pjn.2. mouse.

Organism-specific databases

CTDi170506.
MGIiMGI:1919412. Dhx36.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0920. Eukaryota.
COG1643. LUCA.
GeneTreeiENSGT00760000119189.
HOGENOMiHOG000247063.
HOVERGENiHBG081438.
InParanoidiQ8VHK9.
KOiK14442.
OMAiKRTFRIR.
OrthoDBiEOG7SV0TS.
TreeFamiTF324744.

Enzyme and pathway databases

ReactomeiR-MMU-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-MMU-933541. TRAF6 mediated IRF7 activation.
R-MMU-975110. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.

Miscellaneous databases

ChiTaRSiDhx36. mouse.
NextBioi335597.
PROiQ8VHK9.
SOURCEiSearch...

Gene expression databases

CleanExiMM_DHX36.
GenevisibleiQ8VHK9. MM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
    Strain: C57BL/6J.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-422.
    Tissue: Embryonic tail.
  5. "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 321-1001.
    Strain: C57BL/6J.
    Tissue: Embryo.
  6. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "Histone deacetylase inhibitor MS-275 stimulates bone formation in part by enhancing Dhx36-mediated TNAP transcription."
    Kim H.N., Lee J.H., Bae S.C., Ryoo H.M., Kim H.H., Ha H., Lee Z.H.
    J. Bone Miner. Res. 26:2161-2173(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HDAC1 AND HDAC4.

Entry informationi

Entry nameiDHX36_MOUSE
AccessioniPrimary (citable) accession number: Q8VHK9
Secondary accession number(s): G3X8Y4, Q6ZPP7, Q9CSE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 3, 2012
Last modified: May 11, 2016
This is version 121 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

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.