DHX36
entrez
170506
canonical
uniprot
Q9H2U1
canonical
ensembl
ENSG00000174953
resolver
ensp
ENSP00000330113
resolver
ensp
ENSP00000417078
resolver
genesymbol
DHX36
resolver
genesymbol_syn
DDX36
resolver
genesymbol_syn
KIAA1488
resolver
genesymbol_syn
MLEL1
resolver
genesymbol_syn
RHAU
resolver
hgnc
HGNC:14410
resolver
uniprot
B2RB00
resolver
uniprot
Q70JU3
resolver
uniprot
Q8IYE5
resolver
uniprot
Q9P240
resolver
uniprot_entry
DHX36_HUMAN
resolver
uniprot_sec
B2RB00
resolver
uniprot_sec
Q70JU3
resolver
uniprot_sec
Q8IYE5
resolver
uniprot_sec
Q9P240
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:0000269|PubMed:14731398}.
uniprot
proteins
amino_acid_sequence
MSYDYHQNWGRDGGPRSSGGGYGGGPAGGHGGNRGSGGGGGGGGGGRGGRGRHPGHLKGREIGMWYAKKQGQKNKEAERQERAVVHMDERREEQIVQLLNSVQAKNDKESEAQISWFAPEDHGYGTEVSTKNTPCSENKLDIQEKKLINQEKKMFRIRNRSYIDRDSEYLLQENEPDGTLDQKLLEDLQKKKNDLRYIEMQHFREKLPSYGMQKELVNLIDNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACRIVCTQPRRISAISVAERVAAERAESCGSGNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDPYLSSVSHIVLDEIHERNLQSDVLMTVVKDLLNFRSDLKVILMSATLNAEKFSEYFGNCPMIHIPGFTFPVVEYLLEDVIEKIRYVPEQKEHRSQFKRGFMQGHVNRQEKEEKEAIYKERWPDYVRELRRRYSASTVDVIEMMEDDKVDLNLIVALIRYIVLEEEDGAILVFLPGWDNISTLHDLLMSQVMFKSDKFLIIPLHSLMPTVNQTQVFKRTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYHLYNGLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAYFLSRLMDPPSNEAVLLSIRHLMELNALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLGKEKIADARRKELAKDTRSDHLTVVNAFEGWEEARRRGFRYEKDYCWEYFLSSNTLQMLHNMKGQFAEHLLGAGFVSSRNPKDPESNINSDNEKIIKAVICAGLYPKVAKIRLNLGKKRKMVKVYTKTDGLVAVHPKSVNVEQTDFHYNWLIYHLKMRTSSIYLYDCTEVSPYCLLFFGGDISIQKDNDQETIAVDEWIVFQSPARIAHLVKELRKELDILLQEKIESPHPVDWNDTKSRDCAVLSAIIDLIKTQEKATPRNFPPRFQDGYYS
uniprot
proteins
ec_number
3.6.4.12
uniprot
proteins
ec_number
3.6.4.13
uniprot
proteins
function
FUNCTION: Multifunctional ATP-dependent helicase that unwinds G-quadruplex (G4) structures (PubMed:16150737, PubMed:18854321, PubMed:20472641, PubMed:21586581). Plays a role in many biological processes such as genomic integrity, gene expression regulations and as a sensor to initiate antiviral responses (PubMed:14731398, PubMed:18279852, PubMed:21993297, PubMed:22238380, PubMed:25579584). 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) (PubMed:16150737, PubMed:18842585, PubMed:20472641, PubMed:21586581, PubMed:24369427, PubMed:26195789). Plays a role in genomic integrity (PubMed:22238380). 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 (PubMed:20472641, PubMed:21149580, PubMed:21846770, PubMed:22238380, PubMed:24151078, PubMed:25579584). Plays a role in transcriptional regulation (PubMed:21586581, PubMed:21993297). Resolves G4-DNA structures in promoters of genes, such as YY1, KIT/c-kit and ALPL and positively regulates their expression (PubMed:21993297). Plays a role in post-transcriptional regulation (PubMed:27940037). 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 (PubMed:27940037). 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 (PubMed:24369427, PubMed:26489465). 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 (PubMed:24369427). 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 (PubMed:26489465). Also binds to ARE sequences present in several mRNAs mediating exosome-mediated 3'-5' mRNA degradation (PubMed:14731398, PubMed:18279852). Involved in cytoplasmic urokinase-type plasminogen activator (uPA) mRNA decay (PubMed:14731398). 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 (By similarity). Required for early embryonic development and hematopoiesis. Involved in the regulation of cardioblast differentiation and proliferation during heart development. Involved in spermatogonia differentiation. May play a role in ossification (By similarity). {ECO:0000250|UniProtKB:D4A2Z8, ECO:0000250|UniProtKB:Q05B79, ECO:0000250|UniProtKB:Q8VHK9, ECO:0000269|PubMed:14731398, ECO:0000269|PubMed:16150737, ECO:0000269|PubMed:18279852, ECO:0000269|PubMed:18842585, ECO:0000269|PubMed:18854321, ECO:0000269|PubMed:20472641, ECO:0000269|PubMed:21149580, ECO:0000269|PubMed:21586581, ECO:0000269|PubMed:21846770, ECO:0000269|PubMed:21993297, ECO:0000269|PubMed:22238380, ECO:0000269|PubMed:24151078, ECO:0000269|PubMed:24369427, ECO:0000269|PubMed:25579584, ECO:0000269|PubMed:26195789, ECO:0000269|PubMed:26489465, ECO:0000269|PubMed:27940037}.
uniprot
proteins
mass_dalton
114760
uniprot
proteins
mutagenesis
MUTAGEN 54; /note="P->G: Reduces G4-RNA binding; when associated with A-57, A-59, A-62 and A-63."; /evidence="ECO:0000269|PubMed:20472641"; MUTAGEN 55; /note="G->L: Inhibits G4-DNA-binding; when associated with L-59 and L-63."; /evidence="ECO:0000269|PubMed:26195789"; MUTAGEN 57; /note="L->A: Reduces G4-RNA-binding; when associated with G-54, A-59, A-62 and A-63."; /evidence="ECO:0000269|PubMed:20472641"; MUTAGEN 59; /note="G->A: Reduces G4-RNA-binding; when associated with G-54, A-57, A-62 and A-63."; /evidence="ECO:0000269|PubMed:20472641"; MUTAGEN 59; /note="G->L: Inhibits G4-DNA-binding; when associated with L-55 and L-63."; /evidence="ECO:0000269|PubMed:26195789"; MUTAGEN 59; /note="G->P: Greatly reduces G4-RNA-binding; when associated with P-63."; /evidence="ECO:0000269|PubMed:20472641"; MUTAGEN 62; /note="I->A: Reduces G4-RNA-binding; when associated with G-54, A-57, A-59 and A-63."; /evidence="ECO:0000269|PubMed:20472641"; MUTAGEN 63; /note="G->A: Reduces G4-RNA-binding; when associated with G-54, A-57, A-59 and A-62."; /evidence="ECO:0000269|PubMed:20472641"; MUTAGEN 63; /note="G->L: Inhibits G4-DNA-binding; when associated with L-55 and L-59."; /evidence="ECO:0000269|PubMed:26195789"; MUTAGEN 63; /note="G->P: Greatly reduces G4-RNA-binding; when associated with P-59."; /evidence="ECO:0000269|PubMed:20472641"; MUTAGEN 65; /note="W->A: Does not inhibit G4-DNA-binding; when associated with A-66."; /evidence="ECO:0000269|PubMed:26195789"; MUTAGEN 66; /note="Y->A: Does not inhibit G4-DNA-binding; when associated with A-65."; /evidence="ECO:0000269|PubMed:26195789"; MUTAGEN 335; /note="E->A: Loss of ATPase activity; results in an increased in G4-DNA- and G4-RNA-binding stabilities, increases localization in cytoplasmic stress granules and loss of mRNA deadenylation and mRNA decay."; /evidence="ECO:0000269|PubMed:14731398, ECO:0000269|PubMed:18279852, ECO:0000269|PubMed:18854321, ECO:0000269|PubMed:21846770
uniprot
proteins
protein_family
DEAD box helicase family
uniprot
proteins
protein_family
DEAH subfamily
uniprot
proteins
pubmed
10819331
uniprot
proteins
pubmed
12198572
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14731398
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16150737
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17932509
uniprot
proteins
pubmed
18279852
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18842585
uniprot
proteins
pubmed
18854321
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20472641
uniprot
proteins
pubmed
21149580
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21586581
uniprot
proteins
pubmed
21846770
uniprot
proteins
pubmed
21993297
uniprot
proteins
pubmed
22238380
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24151078
uniprot
proteins
pubmed
24369427
uniprot
proteins
pubmed
25579584
uniprot
proteins
pubmed
26030138
uniprot
proteins
pubmed
26195789
uniprot
proteins
pubmed
26489465
uniprot
proteins
pubmed
26649896
uniprot
proteins
pubmed
27940037
uniprot
proteins
sequence_length
1008
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18279852, ECO:0000269|PubMed:18854321}. Cytoplasm {ECO:0000269|PubMed:18279852, ECO:0000269|PubMed:18854321}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8VHK9}. Cytoplasm, Stress granule {ECO:0000269|PubMed:18854321}. Nucleus speckle {ECO:0000269|PubMed:18279852}. Chromosome, telomere {ECO:0000269|PubMed:20472641}. Mitochondrion {ECO:0000250|UniProtKB:Q8VHK9}. 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 (PubMed:18279852). Colocalizes with SRSF2 in nuclear speckles (PubMed:18279852). Colocalizes with DDX5 in nucleolar caps upon transcription inhibition (PubMed:18279852). Accumulates and colocalized with TIA1 in cytoplasmic stress granules (SGs) in an arsenite-, heat shock- and RNA-binding-dependent manner (PubMed:18854321). Shuttles into and out of SGs in an ATPase-dependent manner (PubMed:18854321). Colocalizes in the cytosol with the multi-helicase-TICAM1 complex that translocates to the mitochondria upon poly(I:C) RNA ligand stimulation (By similarity). {ECO:0000250|UniProtKB:Q8VHK9, ECO:0000269|PubMed:18279852, ECO:0000269|PubMed:18854321}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:14731398}. Cytoplasm {ECO:0000269|PubMed:14731398}. Note=Preferentially localized in the nucleus (PubMed:14731398). Excluded from nucleoli (PubMed:14731398). {ECO:0000269|PubMed:14731398}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:14731398}. Cytoplasm {ECO:0000269|PubMed:14731398}. Note=Preferentially localized in the cytoplasm (PubMed:14731398). Excluded from nucleoli (PubMed:14731398). {ECO:0000269|PubMed:14731398}.
uniprot
proteins