Dhx9
entrez
13211
canonical
uniprot
O70133
canonical
ensembl
ENSMUSG00000042699
resolver
ensp
ENSMUSP00000038135
resolver
ensp
ENSMUSP00000139825
resolver
enst
ENSMUST00000042141
resolver
enst
ENSMUST00000186380
resolver
genesymbol
Dhx9
resolver
genesymbol_syn
Ddx9
resolver
uniprot
A0A087WPL5
resolver
uniprot
E9QNN1
resolver
uniprot
O35931
resolver
uniprot
O54703
resolver
uniprot
Q05BR6
resolver
uniprot
Q3TF92
resolver
uniprot
Q5FWY1
resolver
uniprot
Q6R5F7
resolver
uniprot
Q9CSA2
resolver
uniprot_entry
A0A087WPL5_MOUSE
resolver
uniprot_entry
DHX9_MOUSE
resolver
uniprot_entry
E9QNN1_MOUSE
resolver
uniprot_entry
Q05BR6_MOUSE
resolver
uniprot_entry
Q3TF92_MOUSE
resolver
uniprot_sec
O35931
resolver
uniprot_sec
O54703
resolver
uniprot_sec
Q5FWY1
resolver
uniprot_sec
Q6R5F7
resolver
uniprot_sec
Q9CSA2
resolver
amino_acid_sequence
MGDIKNFLYAWCGKRKMTPAYEIRAVGNKNRQKFMCEVRVEGFNYAGMGNSTNKKDAQSNAARDFVNYLVRINEVKSEEVPAVGIVPPPPILSDTSDSTASAAEGLPAPMGGPLPPHLALKAEENNSGVESSGYGSPGPTWDRGANLKDYYSRKEEQEVQATLESEEVDLNAGLHGNWTLENAKARLNQYFQKEKIQGEYKYTQVGPDHNRSFIAEMTIYIKQLGRRIFAREHGSNKKLAAQSCALSLVRQLYHLGVIEAYSGLTKKKEGERVEPYKVFLSPDLELQLQNVVQELDLEIVPPPVDPSMPVILNIGKLAHFEPSQRQNAVGVVPWSPPQSNWNPWTSSNIDEGPLAYASTEQISMDLKNELTYQMEQDHNLQSVLQERELLPVKKFEAEILEAISSNSVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAVAVAERVAYERGEEPGKSCGYSVRFESILPRPHASIMFCTVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVLAYPEVRIVLMSATIDTTMFCEYFFNCPIIEVYGRTFPVQEYFLEDCIQMTQFIPPPKDKKKKDKEDDGGEDDDANCNLICGDEYGPETKLSMSQLNEKETPFELIEALLKYIETLNVPGAVLVFLPGWNLIYTMQKHLENNSHFGSHRYQILPLHSQIPREEQRKVFDPVPDGVTKVILSTNIAETSITINDVVYVIDSCKQKVKLFTAHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSRARFDRLETHMTPEMFRTPLHEIALSIKLLRLGGIGQFLAKAIEPPPLDAIIEAEHTLRELDALDANDELTPLGRILAKLPIEPRFGKMMIMGCIFYVGDAVCTISAATCFPEPFISEGKRLGYIHRNFAGNRFSDHVALLSVFQAWDDARMSGEEAEIRFCEQKRLNMATLRMTWEAKVQLKEILINSGFPEDCLLTQVFTNTGPDNNLDVVISLLAFGVYPNVCYHKEKRKILTTEGRNALIHKSSVNCPFSSQDMKYPSPFFVFGEKIRTRAISAKGMTLVTPLQLLLFASKKVQSDGQIVFIDDWIRLQISHEAAACITIRAAMEALVVEVSKQPNIISQLDPVNEHMLNTIRQISRPSAAGINLMIGSVRYGDGPRPPKMARYDNGSGYRRGYGGGGYGGGGYGGGYGSGGFGGGFGSGGGFGGGFNSGGGGFGSGGGGFGSGGGGFGGGGGGFSGGGGGGFGGGRGGGGGGFGGSGGFGNGGGGYGVGGGGYGGGGGGGYGGGSGGYGGGGYGGGEGYSISPNSYRGNYGGGGGGYRGGSQGGYRNNFGGDYRGSSGDYRGSGGGYRGSGGFQRRGYGGGYFGQGRGGGGGGGY
uniprot
proteins
ec_number
3.6.4.13
uniprot
proteins
function
FUNCTION: Multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and that plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation and RNA-mediated gene silencing. Requires a 3'-single-stranded tail as entry site for acid nuclei unwinding activities as well as the binding and hydrolyzing of any of the four ribo- or deoxyribo-nucleotide triphosphates (NTPs). Unwinds numerous nucleic acid substrates such as double-stranded (ds) DNA and RNA, DNA:RNA hybrids, DNA and RNA forks composed of either partially complementary DNA duplexes or DNA:RNA hybrids, respectively, and also DNA and RNA displacement loops (D- and R-loops), triplex-helical DNA (H-DNA) structure and DNA- and RNA-based G-quadruplexes. Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing RNA. Also binds to circular dsDNA or dsRNA of either linear and/or circular forms and stimulates the relaxation of supercoiled DNAs catalyzed by topoisomerase TOP2A. Plays a role in DNA replication at origins of replication and cell cycle progression. Plays a role as a transcriptional coactivator acting as a bridging factor between polymerase II holoenzyme and transcription factors or cofactors, such as BRCA1, CREBBP, RELA and SMN1. Binds to the CDKN2A promoter. Plays several roles in post-transcriptional regulation of gene expression. In cooperation with NUP98, promotes pre-mRNA alternative splicing activities of a subset of genes (By similarity). As component of a large PER complex, is involved in the negative regulation of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms (PubMed:22767893). Also acts as a nuclear resolvase that is able to bind and neutralize harmful massive secondary double-stranded RNA structures formed by inverted-repeat Alu retrotransposon elements that are inserted and transcribed as parts of genes during the process of gene transposition (PubMed:28355180). Involved in the positive regulation of nuclear export of constitutive transport element (CTE)-containing unspliced mRNA. Component of the coding region determinant (CRD)-mediated complex that promotes cytoplasmic MYC mRNA stability. Plays a role in mRNA translation. Positively regulates translation of selected mRNAs through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR). Involved with LARP6 in the translation stimulation of type I collagen mRNAs for CO1A1 and CO1A2 through binding of a specific stem-loop structure in their 5'-UTRs. Stimulates LIN28A-dependent mRNA translation probably by facilitating ribonucleoprotein remodeling during the process of translation. Also plays a role as a small interfering (siRNA)-loading factor involved in the RNA-induced silencing complex (RISC) loading complex (RLC) assembly, and hence functions in the RISC-mediated gene silencing process. Binds preferentially to short double-stranded RNA, such as those produced during rotavirus intestinal infection (PubMed:28636595). This interaction may mediate NLRP9 inflammasome activation and trigger inflammatory response, including IL18 release and pyroptosis (PubMed:28636595). Finally, mediates the attachment of heterogeneous nuclear ribonucleoproteins (hnRNPs) to actin filaments in the nucleus (By similarity). {ECO:0000250|UniProtKB:Q08211, ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:28355180, ECO:0000269|PubMed:28636595}.
uniprot
proteins
mass_dalton
149475
uniprot
proteins
mutagenesis
MUTAGEN 416; /note="G->R: Mice show a reduced body size, reduced emotionality, and cardiac conduction abnormalities."; /evidence="ECO:0000269|PubMed:37369308
uniprot
proteins
post_translational_modification
PTM: Methylated. PRMT1-mediated methylation of undefined Arg residues in the nuclear transport domain (NTD) is required for nuclear import of DHX9. {ECO:0000250|UniProtKB:Q08211}.; PTM: Phosphorylated by PRKDC; phosphorylation occurs in a RNA-dependent manner. Phosphorylated by EIF2AK2/PKR; this phosphorylation reduces its association with double-stranded RNA. {ECO:0000250|UniProtKB:Q08211}.
uniprot
proteins
protein_family
DEAD box helicase family
uniprot
proteins
protein_family
DEAH subfamily
uniprot
proteins
pubmed
10413677
uniprot
proteins
pubmed
14691545
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17251188
uniprot
proteins
pubmed
17303075
uniprot
proteins
pubmed
18068128
uniprot
proteins
pubmed
18630941
uniprot
proteins
pubmed
19229320
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22767893
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
28355180
uniprot
proteins
pubmed
28636595
uniprot
proteins
pubmed
37369308
uniprot
proteins
pubmed
37467750
uniprot
proteins
pubmed
9480750
uniprot
proteins
sequence_length
1380
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17303075}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q08211}. Nucleus, nucleolus {ECO:0000269|PubMed:10413677}. Cytoplasm {ECO:0000250|UniProtKB:Q08211}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q08211}. Note=Nucleoplasmic shuttling protein. Its nuclear import involves the nucleocytoplasmic transport receptor Importin alpha/Importin beta receptor pathway in a Ran-dependent manner. In interphase, localizes in nuclear stress granules and at perichromatin fibrils and in cytoplasmic ribonucleoprotein granules. Colocalizes with WRN and H2AX at centrosomes in a microtubule-dependent manner following DNA damaging agent treatment. Excluded from the mitotic nucleus as early as prophase and re-entered the nucleus at telophase. Recruited in diffuse and discrete intranuclear foci (GLFG-body) in a NUP98-dependent manner (By similarity). Colocalizes with SP7 in the nucleus (PubMed:17303075). Colocalizes with ACTB at nuclear actin filaments inside the nucleus or at the nuclear pore. Colocalizes with HNRNPC at nuclear ribonucleoprotein complex proteins in the nucleus. Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). {ECO:0000250|UniProtKB:Q08211, ECO:0000269|PubMed:17303075}.
uniprot
proteins