Dhx36
entrez
72162
canonical
uniprot
Q8VHK9
canonical
ensembl
ENSMUSG00000027770
resolver
ensp
ENSMUSP00000029336
resolver
enst
ENSMUST00000029336
resolver
genesymbol
Dhx36
resolver
genesymbol_syn
Ddx36
resolver
genesymbol_syn
Kiaa1488
resolver
genesymbol_syn
Mlel1
resolver
uniprot
G3X8Y4
resolver
uniprot
Q6ZPP7
resolver
uniprot
Q9CSE8
resolver
uniprot_entry
DHX36_MOUSE
resolver
uniprot_sec
G3X8Y4
resolver
uniprot_sec
Q6ZPP7
resolver
uniprot_sec
Q9CSE8
resolver
activity_regulation
ACTIVITY REGULATION: ATPase activity is enhanced in the presence of homomeric poly(U) RNAs, but not by double-stranded DNA (dsDNA), double-stranded RNA (dsRNA) and tRNA. {ECO:0000250|UniProtKB:Q9H2U1}.
uniprot
proteins
amino_acid_sequence
MSYDYHQSWSRDGGPRGSGQGSSGGGGGGSRGSGGGGGGRGGRGRHPAHLKGREIGLWYAKKQTQKNKEAERQERAVVHMDERREEQIVQLLNSVQAKTDKDSEAQISWFAPEDHGYGTEVSSEKKINSEKKLDNQEKKLLNQEKKTFRITDKSYIDRDSEYLLQENEPNLSLDQHLLEDLQRKKTDPRYIEMQRFRKKLPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACRIVCTQPRRISAISVAERVATERAESCGNGNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMSATLNAEKFSEYFGNCPMIHIPGFTFPVVEYLLEDIIEKIRYVPDQKEHRSQFKRGFMQGHVNRQEKEEKEAIYKERWPAYIKELRTRYSASTVDVLQMMDDDKVDLNLIAALIRYIVLEEEDGAILVFLPGWDNISTLHDLLMSQVMFKSDKFLIIPLHSLMPTVNQTQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYHLYNGLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAYFLSRLMDPPSNEAVVLSIKHLMELSALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLGKEKIADARRKELAKETRSDHLTVVNAFEGWEEAKRRGFRYEKDYCWEYFLSSNTLQMLHNMKGQFAEHLLGAGFVSSRSPKDPKANINSDNEKIIKAVICAGLYPKVAKIRLNLGKKRKMVKVHTKSDGLVSIHPKSVNVEQTDFHYNWLIYHLKMRTSSIYLYDCTEVSPYCLLFFGGDISIQKDKDQEIIAVDEWIVFQSPERIAHLVKGLRKELDSLLQEKIESPHPVDWDDTKSRDCAVLSAILDLIKTQEKATPRNLPPRSQDGYYS
uniprot
proteins
ec_number
3.6.4.13
uniprot
proteins
function
FUNCTION: Multifunctional ATP-dependent helicase that unwinds G-quadruplex (G4) structures (PubMed:25611385). Plays a role in many biological processes such as genomic integrity, gene expression regulations and as a sensor to initiate antiviral responses (PubMed:21590736, PubMed:21703541). G4 structures correspond to helical structures containing guanine tetrads (By similarity). Binds with high affinity to and unwinds G4 structures that are formed in nucleic acids (G4-DNA and G4-RNA) (By similarity). Plays a role in genomic integrity (By similarity). Converts the G4-RNA structure present in telomerase RNA template component (TREC) into a double-stranded RNA to promote P1 helix formation that acts as a template boundary ensuring accurate reverse transcription (By similarity). Plays a role in transcriptional regulation. Resolves G4-DNA structures in promoters of genes, such as YY1, KIT/c-kit and ALPL and positively regulates their expression (By similarity) (PubMed:25611385). Plays a role in post-transcriptional regulation (By similarity). Unwinds a G4-RNA structure located in the 3'-UTR polyadenylation site of the pre-mRNA TP53 and stimulates TP53 pre-mRNA 3'-end processing in response to ultraviolet (UV)-induced DNA damage (By similarity). Binds to the precursor-microRNA-134 (pre-miR-134) terminal loop and regulates its transport into the synapto-dendritic compartment (By similarity). Involved in the pre-miR-134-dependent inhibition of target gene expression and the control of dendritic spine size (By similarity). Plays a role in the regulation of cytoplasmic mRNA translation and mRNA stability (By similarity). Binds to both G4-RNA structures and alternative non-quadruplex-forming sequence within the 3'-UTR of the PITX1 mRNA regulating negatively PITX1 protein expression (By similarity). Binds to both G4-RNA structure in the 5'-UTR and AU-rich elements (AREs) localized in the 3'-UTR of NKX2-5 mRNA to either stimulate protein translation or induce mRNA decay in an ELAVL1-dependent manner, respectively (By similarity). Also binds to ARE sequences present in several mRNAs mediating exosome-mediated 3'-5' mRNA degradation (By similarity). Involved in cytoplasmic urokinase-type plasminogen activator (uPA) mRNA decay (By similarity). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1 (PubMed:21703541). Required for the early embryonic development and hematopoiesis (PubMed:22422825). Involved in the regulation of cardioblast differentiation and proliferation during heart development (PubMed:26489465). Involved in spermatogonia differentiation (PubMed:25611385). May play a role in ossification (PubMed:21590736). {ECO:0000250|UniProtKB:D4A2Z8, ECO:0000250|UniProtKB:Q05B79, ECO:0000250|UniProtKB:Q9H2U1, ECO:0000269|PubMed:21590736, ECO:0000269|PubMed:21703541, ECO:0000269|PubMed:22422825, ECO:0000269|PubMed:25611385, ECO:0000269|PubMed:26489465}.
uniprot
proteins
mass_dalton
113883
uniprot
proteins
protein_family
DEAD box helicase family
uniprot
proteins
protein_family
DEAH subfamily
uniprot
proteins
pubmed
12198572
uniprot
proteins
pubmed
14621295
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16452087
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21590736
uniprot
proteins
pubmed
21703541
uniprot
proteins
pubmed
22422825
uniprot
proteins
pubmed
25611385
uniprot
proteins
pubmed
26489465
uniprot
proteins
sequence_length
1001
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H2U1}. Cytoplasm {ECO:0000250|UniProtKB:Q9H2U1}. Cytoplasm, cytosol {ECO:0000269|PubMed:21703541}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9H2U1}. Nucleus speckle {ECO:0000250|UniProtKB:Q9H2U1}. Chromosome, telomere {ECO:0000250|UniProtKB:Q9H2U1}. Mitochondrion {ECO:0000269|PubMed:21703541}. Perikaryon {ECO:0000250|UniProtKB:D4A2Z8}. Cell projection, dendrite {ECO:0000250|UniProtKB:D4A2Z8}. Cell projection, axon {ECO:0000250|UniProtKB:D4A2Z8}. Note=Predominantly localized in the nucleus. Colocalizes with SRSF2 in nuclear speckles. Colocalizes with DDX5 in nucleolar caps upon transcription inhibition. Accumulates and colocalized with TIA1 in cytoplasmic stress granules (SGs) in an arsenite-, heat shock- and RNA-binding-dependent manner. Shuttles into and out of SGs in an ATPase-dependent manner (By similarity). Colocalizes in the cytosol with the multi-helicase-TICAM1 complex that translocates to the mitochondria upon poly(I:C) stimulation (PubMed:21703541). {ECO:0000250|UniProtKB:Q9H2U1, ECO:0000269|PubMed:21703541}.
uniprot
proteins