DHX9
entrez
1660
canonical
uniprot
Q08211
canonical
ensembl
ENSG00000135829
resolver
ensp
ENSP00000356520
resolver
genesymbol
DHX9
resolver
genesymbol_syn
DDX9
resolver
genesymbol_syn
LKP
resolver
genesymbol_syn
NDH2
resolver
hgnc
HGNC:2750
resolver
uniprot
B2RNV4
resolver
uniprot
B3KU66
resolver
uniprot
Q05CI5
resolver
uniprot
Q12803
resolver
uniprot
Q32Q22
resolver
uniprot
Q5VY62
resolver
uniprot
Q6PD69
resolver
uniprot
Q99556
resolver
uniprot_entry
B3KU66_HUMAN
resolver
uniprot_entry
DHX9_HUMAN
resolver
uniprot_sec
B2RNV4
resolver
uniprot_sec
Q05CI5
resolver
uniprot_sec
Q12803
resolver
uniprot_sec
Q32Q22
resolver
uniprot_sec
Q5VY62
resolver
uniprot_sec
Q6PD69
resolver
uniprot_sec
Q99556
resolver
amino_acid_sequence
MGDVKNFLYAWCGKRKMTPSYEIRAVGNKNRQKFMCEVQVEGYNYTGMGNSTNKKDAQSNAARDFVNYLVRINEIKSEEVPAFGVASPPPLTDTPDTTANAEGDLPTTMGGPLPPHLALKAENNSEVGASGYGVPGPTWDRGANLKDYYSRKEEQEVQATLESEEVDLNAGLHGNWTLENAKARLNQYFQKEKIQGEYKYTQVGPDHNRSFIAEMTIYIKQLGRRIFAREHGSNKKLAAQSCALSLVRQLYHLGVVEAYSGLTKKKEGETVEPYKVNLSQDLEHQLQNIIQELNLEILPPPEDPSVPVALNIGKLAQFEPSQRQNQVGVVPWSPPQSNWNPWTSSNIDEGPLAFATPEQISMDLKNELMYQLEQDHDLQAILQERELLPVKKFESEILEAISQNSVVIIRGATGCGKTTQVPQFILDDFIQNDRAAECNIVVTQPRRISAVSVAERVAFERGEEPGKSCGYSVRFESILPRPHASIMFCTVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPEVRIVLMSATIDTSMFCEYFFNCPIIEVYGRTYPVQEYFLEDCIQMTHFVPPPKDKKKKDKDDDGGEDDDANCNLICGDEYGPETRLSMSQLNEKETPFELIEALLKYIETLNVPGAVLVFLPGWNLIYTMQKHLEMNPHFGSHRYQILPLHSQIPREEQRKVFDPVPVGVTKVILSTNIAETSITINDVVYVIDSCKQKVKLFTAHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSRARFERLETHMTPEMFRTPLHEIALSIKLLRLGGIGQFLAKAIEPPPLDAVIEAEHTLRELDALDANDELTPLGRILAKLPIEPRFGKMMIMGCIFYVGDAICTIAAATCFPEPFINEGKRLGYIHRNFAGNRFSDHVALLSVFQAWDDARMGGEEAEIRFCEHKRLNMATLRMTWEAKVQLKEILINSGFPEDCLLTQVFTNTGPDNNLDVVISLLAFGVYPNVCYHKEKRKILTTEGRNALIHKSSVNCPFSSQDMKYPSPFFVFGEKIRTRAISAKGMTLVTPLQLLLFASKKVQSDGQIVLVDDWIKLQISHEAAACITGLRAAMEALVVEVTKQPAIISQLDPVNERMLNMIRQISRPSAAGINLMIGSTRYGDGPRPPKMARYDNGSGYRRGGSSYSGGGYGGGYSSGGYGSGGYGGSANSFRAGYGAGVGGGYRGVSRGGFRGNSGGDYRGPSGGYRGSGGFQRGGGRGAYGTGYFGQGRGGGGY
uniprot
proteins
disease_involvement
DISEASE: Intellectual developmental disorder, autosomal dominant 75 (MRD75) [MIM:620988]: An autosomal dominant neurodevelopmental disorder characterized by developmental delay, mild to severe impaired intellectual development, and neuropsychiatric manifestations including autism spectrum disorder, anxiety, and obsessive compulsive disorder. Disease features are highly variable and may include hypotonia, seizures, non-specific dysmorphism, poor overall growth with small head circumference, abnormal brain imaging, and heart disease. {ECO:0000269|PubMed:37369308, ECO:0000269|PubMed:37467750}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (PubMed:11416126, PubMed:12711669, PubMed:15355351, PubMed:16680162, PubMed:17531811, PubMed:20669935, PubMed:21561811, PubMed:24049074, PubMed:24990949, PubMed:25062910, PubMed:28221134, PubMed:9111062, PubMed:37467750). 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) (PubMed:1537828). 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 (PubMed:20669935, PubMed:21561811, PubMed:24049074). Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing RNA (PubMed:10198287, PubMed:9111062). 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 (PubMed:12711669). Plays a role in DNA replication at origins of replication and cell cycle progression (PubMed:24990949). 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 (PubMed:11038348, PubMed:11149922, PubMed:11416126, PubMed:15355351, PubMed:28221134, PubMed:9323138, PubMed:9662397). Binds to the CDKN2A promoter (PubMed:11038348). Plays several roles in post-transcriptional regulation of gene expression (PubMed:28221134, PubMed:28355180). In cooperation with NUP98, promotes pre-mRNA alternative splicing activities of a subset of genes (PubMed:11402034, PubMed:16680162, PubMed:28221134, PubMed:28355180). 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 (By similarity). 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 (PubMed:10924507, PubMed:11402034, PubMed:9162007). Component of the coding region determinant (CRD)-mediated complex that promotes cytoplasmic MYC mRNA stability (PubMed:19029303). Plays a role in mRNA translation (PubMed:28355180). Positively regulates translation of selected mRNAs through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR) (PubMed:16680162). 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 (PubMed:22190748). Stimulates LIN28A-dependent mRNA translation probably by facilitating ribonucleoprotein remodeling during the process of translation (PubMed:21247876). Plays also 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 (PubMed:17531811). 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 (PubMed:11687588). {ECO:0000250|UniProtKB:O70133, ECO:0000269|PubMed:10198287, ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:11038348, ECO:0000269|PubMed:11149922, ECO:0000269|PubMed:11402034, ECO:0000269|PubMed:11416126, ECO:0000269|PubMed:11687588, ECO:0000269|PubMed:12711669, ECO:0000269|PubMed:15355351, ECO:0000269|PubMed:1537828, ECO:0000269|PubMed:16680162, ECO:0000269|PubMed:17531811, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:20669935, ECO:0000269|PubMed:21247876, ECO:0000269|PubMed:21561811, ECO:0000269|PubMed:22190748, ECO:0000269|PubMed:24049074, ECO:0000269|PubMed:24990949, ECO:0000269|PubMed:25062910, ECO:0000269|PubMed:28221134, ECO:0000269|PubMed:28355180, ECO:0000269|PubMed:28636595, ECO:0000269|PubMed:37467750, ECO:0000269|PubMed:9111062, ECO:0000269|PubMed:9162007, ECO:0000269|PubMed:9323138, ECO:0000269|PubMed:9662397}.; FUNCTION: (Microbial infection) Plays a role in HIV-1 replication and virion infectivity (PubMed:11096080, PubMed:19229320, PubMed:25149208, PubMed:27107641). Enhances HIV-1 transcription by facilitating the binding of RNA polymerase II holoenzyme to the proviral DNA (PubMed:11096080, PubMed:25149208). Binds (via DRBM domain 2) to the HIV-1 TAR RNA and stimulates HIV-1 transcription of transactivation response element (TAR)-containing mRNAs (PubMed:11096080, PubMed:9892698). Involved also in HIV-1 mRNA splicing and transport (PubMed:25149208). Positively regulates HIV-1 gag mRNA translation, through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR) (PubMed:16680162). Binds (via DRBM domains) to a HIV-1 double-stranded RNA region of the primer binding site (PBS)-segment of the 5'-UTR, and hence stimulates DHX9 incorporation into virions and virion infectivity (PubMed:27107641). Also plays a role as a cytosolic viral MyD88-dependent DNA and RNA sensors in plasmacytoid dendritic cells (pDCs), and hence induce antiviral innate immune responses (PubMed:20696886, PubMed:21957149). Binds (via the OB-fold region) to viral single-stranded DNA unmethylated C-phosphate-G (CpG) oligonucleotide (PubMed:20696886). {ECO:0000269|PubMed:11096080, ECO:0000269|PubMed:16680162, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:20696886, ECO:0000269|PubMed:21957149, ECO:0000269|PubMed:25149208, ECO:0000269|PubMed:27107641, ECO:0000269|PubMed:9892698}.
uniprot
proteins
mass_dalton
140958
uniprot
proteins
mutagenesis
MUTAGEN 5; /note="K->A: Reduces siRNA-binding and interaction with AGO2; when associated with A-6."; /evidence="ECO:0000269|PubMed:23361462"; MUTAGEN 6; /note="N->A: Reduces siRNA-binding; when associated with A-5."; /evidence="ECO:0000269|PubMed:23361462"; MUTAGEN 9; /note="Y->A: Inhibits siRNA-binding and interaction with AGO2."; /evidence="ECO:0000269|PubMed:23361462"; MUTAGEN 30; /note="N->A: Does not reduce siRNA-binding and interaction with AGO2."; /evidence="ECO:0000269|PubMed:23361462"; MUTAGEN 53; /note="N->A: Inhibits siRNA-binding and decreases interaction with AGO2; when associated with A-54 and A-55."; /evidence="ECO:0000269|PubMed:23361462"; MUTAGEN 54; /note="K->A: Inhibits siRNA-binding and decreases interaction with AGO2; when associated with A-53 and A-55."; /evidence="ECO:0000269|PubMed:23361462"; MUTAGEN 55; /note="K->A: Inhibits siRNA-binding and decreases interaction with AGO2; when associated with A-53 and A-54."; /evidence="ECO:0000269|PubMed:23361462"; MUTAGEN 182; /note="K->A: Reduces siRNA-binding and interaction with AGO2."; /evidence="ECO:0000269|PubMed:23361462"; MUTAGEN 186; /note="N->A: Reduces siRNA-binding and interaction with AGO2; when associated with A-187."; /evidence="ECO:0000269|PubMed:23361462"; MUTAGEN 187; /note="Q->A: Reduces siRNA-binding and interaction with AGO2; when associated with A-186."; /evidence="ECO:0000269|PubMed:23361462"; MUTAGEN 207; /note="H->A: Reduces siRNA-binding and interaction with AGO2."; /evidence="ECO:0000269|PubMed:23361462"; MUTAGEN 234; /note="N->A: Inhibits siRNA-binding and interaction with AGO2; when associated with A-235 and A-236."; /evidence="ECO:0000269|PubMed:23361462"; MUTAGEN 235; /note="K->A: Inhibits siRNA-binding and interaction with AGO2; when associated with A-234 and A-236."; /evidence="ECO:0000269|PubMed:23361462"; MUTAGEN 236; /note="K->A: Inhibits siRNA-binding and interaction with AGO2; when associated with A-234 and A-235."; /evidence="ECO:0000269|PubMed:23361462"; MUTAGEN 332; /note="W->A: Abrogates transcriptional activation by the MTAD region. No change in RNA polymerase II holoenzyme binding."; /evidence="ECO:0000269|PubMed:11416126"; MUTAGEN 339; /note="W->A: Abrogates transcriptional activation and RNA polymerase II binding by the MTAD region. No change in ATP binding and ATPase activities."; /evidence="ECO:0000269|PubMed:11416126"; MUTAGEN 342; /note="W->A: Abrogates transcriptional activation by the MTAD region. No change in RNA polymerase II holoenzyme binding."; /evidence="ECO:0000269|PubMed:11416126"; MUTAGEN 347; /note="I->A: Reduces NUP98-induced mRNA transcription and alternative splicing activities."; /evidence="ECO:0000269|PubMed:28221134"; MUTAGEN 417; /note="K->R,N: Inhibits interaction with AGO2, DICER1 and TARBP2. Abrogates helicase activity and transcriptional activation. Does not inhibit binding to origins of DNA replication."; /evidence="ECO:0000269|PubMed:15355351, ECO:0000269|PubMed:17531811, ECO:0000269|PubMed:24990949, ECO:0000269|PubMed:9323138"; MUTAGEN 417; /note="K->R: Reduces NUP98-induced mRNA transcription and alternative splicing activities."; /evidence="ECO:0000269|PubMed:28221134"; MUTAGEN 511; /note="D->A: Does not inhibit binding to origins of DNA replication; when associated with A-512."; /evidence="ECO:0000269|PubMed:24990949"; MUTAGEN 512; /note="E->A: Does not inhibit binding to origins of DNA replication; when associated with A-511."; /evidence="ECO:0000269|PubMed:24990949"; MUTAGEN 543; /note="S->L: Does not inhibit binding to origins of DNA replication."; /evidence="ECO:0000269|PubMed:24990949"; MUTAGEN 1160; /note="R->A: Localizes in the nucleus and interacts with the importin complex."; /evidence="ECO:0000269|PubMed:16375861"; MUTAGEN 1163; /note="K->A: Localizes in the cytoplasm and does not interact with the importin complex."; /evidence="ECO:0000269|PubMed:16375861"; MUTAGEN 1163; /note="Missing: Abolishes nuclear localization."; /evidence="ECO:0000269|PubMed:10207077"; MUTAGEN 1166; /note="R->A: Localizes in the nucleus and the cytoplasm and interacts weakly with the importin complex."; /evidence="ECO:0000269|PubMed:16375861"; MUTAGEN 1166; /note="R->L: Abolishes nuclear localization."; /evidence="ECO:0000269|PubMed:10207077"; MUTAGEN 1166; /note="Missing: Abolishes nuclear localization."; /evidence="ECO:0000269|PubMed:10207077
uniprot
proteins
post_translational_modification
PTM: Methylated (PubMed:15084609). PRMT1-mediated methylation of undefined Arg residues in the RGG region is required for nuclear import of DHX9 (PubMed:15084609). {ECO:0000269|PubMed:15084609}.; PTM: Phosphorylated by PRKDC; phosphorylation occurs in a RNA-dependent manner (PubMed:14704337). Phosphorylated by EIF2AK2/PKR; this phosphorylation reduces its association with double-stranded RNA (PubMed:19229320). {ECO:0000269|PubMed:14704337, ECO:0000269|PubMed:19229320}.
uniprot
proteins
protein_family
DEAD box helicase family
uniprot
proteins
protein_family
DEAH subfamily
uniprot
proteins
pubmed
10198287
uniprot
proteins
pubmed
10207077
uniprot
proteins
pubmed
10924507
uniprot
proteins
pubmed
11038348
uniprot
proteins
pubmed
11096080
uniprot
proteins
pubmed
11149922
uniprot
proteins
pubmed
11402034
uniprot
proteins
pubmed
11416126
uniprot
proteins
pubmed
11687588
uniprot
proteins
pubmed
12429849
uniprot
proteins
pubmed
12665568
uniprot
proteins
pubmed
12711669
uniprot
proteins
pubmed
12946349
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14704337
uniprot
proteins
pubmed
15084609
uniprot
proteins
pubmed
15355351
uniprot
proteins
pubmed
1537828
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15613478
uniprot
proteins
pubmed
15995249
uniprot
proteins
pubmed
16375861
uniprot
proteins
pubmed
16680162
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17251188
uniprot
proteins
pubmed
17289661
uniprot
proteins
pubmed
17303075
uniprot
proteins
pubmed
17498979
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17531811
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19029303
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19229320
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20510246
uniprot
proteins
pubmed
20669935
uniprot
proteins
pubmed
20696886
uniprot
proteins
pubmed
21247876
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21561811
uniprot
proteins
pubmed
21957149
uniprot
proteins
pubmed
22190748
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23308148
uniprot
proteins
pubmed
23361462
uniprot
proteins
pubmed
23640942
uniprot
proteins
pubmed
23652018
uniprot
proteins
pubmed
24049074
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24990949
uniprot
proteins
pubmed
25062910
uniprot
proteins
pubmed
25149208
uniprot
proteins
pubmed
27107641
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28221134
uniprot
proteins
pubmed
28355180
uniprot
proteins
pubmed
28636595
uniprot
proteins
pubmed
30463980
uniprot
proteins
pubmed
30541834
uniprot
proteins
pubmed
37369308
uniprot
proteins
pubmed
37467750
uniprot
proteins
pubmed
8344961
uniprot
proteins
pubmed
8690889
uniprot
proteins
pubmed
9111062
uniprot
proteins
pubmed
9162007
uniprot
proteins
pubmed
9323138
uniprot
proteins
pubmed
9662397
uniprot
proteins
pubmed
9892698
uniprot
proteins
sequence_length
1270
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10198287, ECO:0000269|PubMed:10207077, ECO:0000269|PubMed:11687588, ECO:0000269|PubMed:16375861, ECO:0000269|PubMed:17303075, ECO:0000269|PubMed:37467750, ECO:0000269|PubMed:9162007}. Nucleus, nucleoplasm {ECO:0000269|PubMed:28221134}. Nucleus, nucleolus {ECO:0000269|PubMed:12429849}. Cytoplasm {ECO:0000269|PubMed:10198287, ECO:0000269|PubMed:10207077, ECO:0000269|PubMed:16375861, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:20696886, ECO:0000269|PubMed:8690889, ECO:0000269|PubMed:9162007}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:17498979}. Note=Nucleoplasmic shuttling protein (PubMed:10198287, PubMed:10207077, PubMed:16375861, PubMed:9162007). Its nuclear import involves the nucleocytoplasmic transport receptor Importin alpha/Importin beta receptor pathway in a Ran-dependent manner (PubMed:16375861). In interphase, localizes in nuclear stress granules and at perichromatin fibrils and in cytoplasmic ribonucleoprotein granules (PubMed:10198287). Colocalizes with WRN and H2AX at centrosomes in a microtubule-dependent manner following DNA damaging agent treatment (PubMed:17498979). Excluded from the mitotic nucleus as early as prophase and re-entered the nucleus at telophase (PubMed:10198287). Recruited in diffuse and discrete intranuclear foci (GLFG-body) in a NUP98-dependent manner (PubMed:28221134). Colocalizes with SP7 in the nucleus (PubMed:17303075). Colocalizes with ACTB at nuclear actin filaments inside the nucleus or at the nuclear pore (PubMed:11687588). Colocalizes with HNRNPC at nuclear ribonucleoprotein complex proteins in the nucleus (PubMed:11687588). Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661). {ECO:0000269|PubMed:10198287, ECO:0000269|PubMed:10207077, ECO:0000269|PubMed:11687588, ECO:0000269|PubMed:16375861, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17303075, ECO:0000269|PubMed:17498979, ECO:0000269|PubMed:28221134, ECO:0000269|PubMed:9162007}.
uniprot
proteins