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Protein

ATP-dependent RNA helicase A

Gene

Dhx9

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

Functioni

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. Binds also 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). Acts also 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. 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. 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).By similarity3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi420ManganeseBy similarity1
Metal bindingi514ManganeseBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi413 – 421ATPPROSITE-ProRule annotationBy similarity9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding, Helicase, Hydrolase, RNA-binding
Biological processBiological rhythms, Immunity, Inflammatory response, Innate immunity, mRNA processing, mRNA splicing, mRNA transport, RNA-mediated gene silencing, Transcription, Transcription regulation, Transcription termination, Translation regulation, Transport
LigandATP-binding, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase ABy similarity (EC:3.6.4.13By similarity)
Alternative name(s):
DEAH box protein 91 Publication
Short name:
mHEL-51 Publication
Nuclear DNA helicase IIBy similarity
Short name:
NDH IIBy similarity
RNA helicase A1 Publication
Short name:
RHA1 Publication
Gene namesi
Name:Dhx9Imported
Synonyms:Ddx9By similarity
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:108177. Dhx9.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000551581 – 1380ATP-dependent RNA helicase AAdd BLAST1380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei127PhosphoserineBy similarity1
Modified residuei136PhosphoserineCombined sources1
Modified residuei148N6-acetyllysine; alternateCombined sources1
Modified residuei148N6-methyllysine; alternateBy similarity1
Modified residuei193N6-acetyllysineBy similarity1
Modified residuei201N6-acetyllysineBy similarity1
Modified residuei323PhosphoserineBy similarity1
Modified residuei451PhosphoserineBy similarity1
Modified residuei508PhosphoserineBy similarity1
Cross-linki699Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1026N6-acetyllysineBy similarity1
Modified residuei1167Asymmetric dimethylarginineCombined sources1
Modified residuei1176Omega-N-methylarginineBy similarity1
Modified residuei1312Asymmetric dimethylarginineCombined sources1
Modified residuei1323Asymmetric dimethylarginineCombined sources1
Modified residuei1339Asymmetric dimethylarginineCombined sources1
Modified residuei1346Asymmetric dimethylarginineCombined sources1
Modified residuei1353Asymmetric dimethylarginineCombined sources1
Modified residuei1361Asymmetric dimethylarginineCombined sources1
Modified residuei1372Asymmetric dimethylarginineCombined sources1
Isoform 2 (identifier: O70133-2)
Modified residuei137PhosphoserineCombined sources1

Post-translational modificationi

Methylated. PRMT1-mediated methylation of undefined Arg residues in the nuclear transport domain (NTD) is required for nuclear import of DHX9.By similarity
Phosphorylated by PRKDC; phosphorylation occurs in a RNA-dependent manner. Phosphorylated by EIF2AK2/PKR; this phosphorylation reduces its association with double-stranded RNA.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO70133.
MaxQBiO70133.
PaxDbiO70133.
PeptideAtlasiO70133.
PRIDEiO70133.

PTM databases

iPTMnetiO70133.
PhosphoSitePlusiO70133.
SwissPalmiO70133.

Expressioni

Gene expression databases

CleanExiMM_DHX9.

Interactioni

Subunit structurei

Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (By similarity). The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active) (PubMed:22767893). Associates (via DRBM domains) with the RISC complex; this association occurs in a small interfering (siRNA)-dependent manner. Associates with the SMN complex; this association induces recruitment of DHX9 to the RNA polymerase II. Associates with polysomes in a LIN28A-dependent manner. Interacts (via C-terminus) with ACTB; this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes (By similarity). Interacts with ADAR isoform 1; this interaction occurs in a RNA-independent manner (PubMed:28355180). Interacts (via DRBM domains) with AGO2 (via middle region); this interaction promotes active RISC assembly by promoting the association of siRNA with AGO2. Interacts (via NTD domain) with AKAP8L (via N-terminus). Interacts with BRCA1 (via C-terminus); this interaction is direct and links BRCA1 to the RNA polymerase II holoenzyme. Interacts (via N-terminus) with CREBBP; this interaction mediates association with RNA polymerase II holoenzyme and stimulates CREB-dependent transcriptional activation (By similarity). Interacts (via N-terminus) with EIF2AK2/PKR; this interaction is dependent upon the activation of the kinase (PubMed:19229320). Interacts (via DRBM domains) with DICER1. Interacts with H2AFX; this interaction is direct, requires phosphorylation of histone H2AFX on 'Ser-140' by PRKDC and promotes binding of DHX9 to transcriptionally stalled sites on chromosomal DNA in response to genotoxic stress. Interacts with HNRNPC; this interaction is direct, enhanced probably by their concomitant binding to RNA and mediates the attachment to actin filaments. Interacts (via NTD domain) with PRMT1. Interacts with IGF2BP1. Interacts with IGF2BP2, IGF2BP3. Interacts (via DRBM domains) with ILF3; this interaction occurs in a RNA-independent manner. Interacts with Importin alpha/Importin beta receptor. Interacts with LARP6 (via C-terminus); this interaction occurs in a mRNA-independent manner. Interacts (via N- and C-terminus) with LIN28A (via C-terminus); this interaction occurs in a RNA-independent manner. Interacts with LMX1B. Interacts (via helicase C-terminal domain, HA2 and OB-fold regions) with MAVS (via CARD domain); this interaction occurs in both resting and double-stranded RNA poly(I:C)-induced cells. Interacts with MBD2; this interaction stimulates transcriptional activation in a CREB-dependent manner. Interacts (via H2A and OB-fold regions) with MYD88 (via TIR domain); this interaction is direct. Interacts with NLRP9 upon rotavirus infection; this interaction may trigger NLRP9 inflammasome activation and inflammatory response. Interacts (via DRBM, OB-fold and RGG regions) with NUP98 (via N-terminus); this interaction occurs in a RNA-dependent manner and stimulates DHX9-mediated ATPase activity and regulates transcription and splicing of a subset of genes. Interacts (via N-terminus) with NXF1 (via N-terminus); this interaction is direct and negatively regulates NXF1-mediated nuclear export of constitutive transport element (CTE)-containing cellular mRNAs. Interacts with RELA; this interaction is direct and activates NF-kappa-B-mediated transcription. Interacts (via MTAD region) with RNA polymerase II holoenzyme; this interaction stimulates transcription activation in a CREB-dependent manner. Interacts (via RGG region) with SMN1; this interaction links SMN1 to the RNA polymerase II holoenzyme (By similarity). Interacts with SP7 (PubMed:17303075). Interacts (via DRBM domains) with TARBP2 (via DRBM first and second domains); this interaction occurs in a small interfering (siRNA)-dependent manner. Interacts with TOP2A; this interaction occurs in a E2 enzyme UBE2I- and RNA-dependent manner, negatively regulates DHX9-mediated double-stranded DNA and RNA duplex helicase activity and stimulates TOP2A-mediated supercoiled DNA relaxation activity. Interacts (via DRBM domains and C-terminus) with WRN (via 3'-5' exonuclease domain); this interaction inhibits the DNA-dependent NTPase and DNA helicase activities of DHX9 and stimulates the 3'-5' exonuclease activity of WRN. Interacts with XRCC5; this interaction occurs in a RNA-dependent manner (By similarity). Interacts with ZIC2 (via C2H2-type domain 3) (PubMed:17251188).By similarity5 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199088. 8 interactors.
IntActiO70133. 10 interactors.
MINTiMINT-1868227.
STRINGi10090.ENSMUSP00000038135.

Structurei

Secondary structure

11380
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 14Combined sources10
Beta strandi20 – 27Combined sources8
Beta strandi29 – 39Combined sources11
Beta strandi47 – 53Combined sources7
Helixi54 – 72Combined sources19
Turni77 – 79Combined sources3
Helixi172 – 175Combined sources4
Helixi180 – 193Combined sources14
Beta strandi201 – 206Combined sources6
Beta strandi212 – 221Combined sources10
Turni222 – 225Combined sources4
Beta strandi226 – 231Combined sources6
Helixi237 – 255Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UILNMR-A163-262[»]
1WHQNMR-A4-89[»]
2RS6NMR-A4-89[»]
2RS7NMR-A163-262[»]
ProteinModelPortaliO70133.
SMRiO70133.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO70133.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 71DRBM 1PROSITE-ProRule annotationBy similarityAdd BLAST69
Domaini182 – 254DRBM 2PROSITE-ProRule annotationBy similarityAdd BLAST73
Domaini400 – 566Helicase ATP-bindingPROSITE-ProRule annotationBy similarityAdd BLAST167
Domaini638 – 811Helicase C-terminalPROSITE-ProRule annotationAdd BLAST174

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 252Interaction with CREBBPBy similarityAdd BLAST252
Regioni5 – 9siRNA-bindingBy similarity5
Regioni53 – 55siRNA-bindingBy similarity3
Regioni184 – 188siRNA-bindingBy similarity5
Regioni232 – 327Interaction with BRCA1By similarityAdd BLAST96
Regioni236 – 238siRNA-bindingBy similarity3
Regioni257 – 666Necessary for interaction with RNA polymerase II holoenzymeBy similarityAdd BLAST410
Regioni315 – 954Necessary for interaction with H2AFXBy similarityAdd BLAST640
Regioni333 – 382MTADBy similarityAdd BLAST50
Regioni400 – 811Core helicaseBy similarityAdd BLAST412
Regioni833 – 921HA2By similarityAdd BLAST89
Regioni960 – 1076OB-foldBy similarityAdd BLAST117
Regioni1151 – 1366NTD regionBy similarityAdd BLAST216
Regioni1152 – 1380RGGBy similarityAdd BLAST229

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi513 – 516DEAH box4
Motifi588 – 597Nuclear localization signal (NLS1)Sequence analysis10
Motifi1156 – 1174Nuclear localization signal (NLS2)By similarityAdd BLAST19

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1171 – 1380Arg/Gly/Ser/Tyr-richAdd BLAST210

Domaini

DRBM domains cooperate for the binding to nucleic acid but not for unwinding helicase activity. The helicase-associated domain-2 (HA2) region is essential for the duplex RNA unwinding helicase activity. The minimal transactivation region (MTAD) mediates interaction with the RNA polymerase II holoenzyme and stimulates transcriptional activation in a CREB-dependent manner. The oligonucleotide- or oligosaccharide-binding (OB-fold) and the repeated arginine and glycine-glycine (RGG) regions are dispensable for both RNA-binding and unwinding helicase activities. The RGG region contains both nuclear localization signal (NLS) and nuclear export signal (NES) and is necessary and sufficient for nucleocytoplasmic shuttling in a RNA-independent manner.By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0920. Eukaryota.
COG1643. LUCA.
HOGENOMiHOG000247063.
HOVERGENiHBG039429.
InParanoidiO70133.
KOiK13184.
PhylomeDBiO70133.

Family and domain databases

CDDicd00079. HELICc. 1 hit.
InterProiView protein in InterPro
IPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR014720. dsRBD_dom.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
PfamiView protein in Pfam
PF00270. DEAD. 1 hit.
PF00035. dsrm. 2 hits.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
SMARTiView protein in SMART
SM00487. DEXDc. 1 hit.
SM00358. DSRM. 2 hits.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiView protein in PROSITE
PS00690. DEAH_ATP_HELICASE. 1 hit.
PS50137. DS_RBD. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O70133-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGDIKNFLYA WCGKRKMTPA YEIRAVGNKN RQKFMCEVRV EGFNYAGMGN
60 70 80 90 100
STNKKDAQSN AARDFVNYLV RINEVKSEEV PAVGIVPPPP ILSDTSDSTA
110 120 130 140 150
SAAEGLPAPM GGPLPPHLAL KAEENNSGVE SSGYGSPGPT WDRGANLKDY
160 170 180 190 200
YSRKEEQEVQ ATLESEEVDL NAGLHGNWTL ENAKARLNQY FQKEKIQGEY
210 220 230 240 250
KYTQVGPDHN RSFIAEMTIY IKQLGRRIFA REHGSNKKLA AQSCALSLVR
260 270 280 290 300
QLYHLGVIEA YSGLTKKKEG ERVEPYKVFL SPDLELQLQN VVQELDLEIV
310 320 330 340 350
PPPVDPSMPV ILNIGKLAHF EPSQRQNAVG VVPWSPPQSN WNPWTSSNID
360 370 380 390 400
EGPLAYASTE QISMDLKNEL TYQMEQDHNL QSVLQERELL PVKKFEAEIL
410 420 430 440 450
EAISSNSVVI IRGATGCGKT TQVPQYILDD FIQNDRAAEC NIVVTQPRRI
460 470 480 490 500
SAVAVAERVA YERGEEPGKS CGYSVRFESI LPRPHASIMF CTVGVLLRKL
510 520 530 540 550
EAGIRGISHV IVDEIHERDI NTDFLLVVLR DVVLAYPEVR IVLMSATIDT
560 570 580 590 600
TMFCEYFFNC PIIEVYGRTF PVQEYFLEDC IQMTQFIPPP KDKKKKDKED
610 620 630 640 650
DGGEDDDANC NLICGDEYGP ETKLSMSQLN EKETPFELIE ALLKYIETLN
660 670 680 690 700
VPGAVLVFLP GWNLIYTMQK HLENNSHFGS HRYQILPLHS QIPREEQRKV
710 720 730 740 750
FDPVPDGVTK VILSTNIAET SITINDVVYV IDSCKQKVKL FTAHNNMTNY
760 770 780 790 800
ATVWASKTNL EQRKGRAGRV RPGFCFHLCS RARFDRLETH MTPEMFRTPL
810 820 830 840 850
HEIALSIKLL RLGGIGQFLA KAIEPPPLDA IIEAEHTLRE LDALDANDEL
860 870 880 890 900
TPLGRILAKL PIEPRFGKMM IMGCIFYVGD AVCTISAATC FPEPFISEGK
910 920 930 940 950
RLGYIHRNFA GNRFSDHVAL LSVFQAWDDA RMSGEEAEIR FCEQKRLNMA
960 970 980 990 1000
TLRMTWEAKV QLKEILINSG FPEDCLLTQV FTNTGPDNNL DVVISLLAFG
1010 1020 1030 1040 1050
VYPNVCYHKE KRKILTTEGR NALIHKSSVN CPFSSQDMKY PSPFFVFGEK
1060 1070 1080 1090 1100
IRTRAISAKG MTLVTPLQLL LFASKKVQSD GQIVFIDDWI RLQISHEAAA
1110 1120 1130 1140 1150
CITIRAAMEA LVVEVSKQPN IISQLDPVNE HMLNTIRQIS RPSAAGINLM
1160 1170 1180 1190 1200
IGSVRYGDGP RPPKMARYDN GSGYRRGYGG GGYGGGGYGG GYGSGGFGGG
1210 1220 1230 1240 1250
FGSGGGFGGG FNSGGGGFGS GGGGFGSGGG GFGGGGGGFS GGGGGGFGGG
1260 1270 1280 1290 1300
RGGGGGGFGG SGGFGNGGGG YGVGGGGYGG GGGGGYGGGS GGYGGGGYGG
1310 1320 1330 1340 1350
GEGYSISPNS YRGNYGGGGG GYRGGSQGGY RNNFGGDYRG SSGDYRGSGG
1360 1370 1380
GYRGSGGFQR RGYGGGYFGQ GRGGGGGGGY
Length:1,380
Mass (Da):149,475
Last modified:July 19, 2005 - v2
Checksum:i005D641CD9A4F0C9
GO
Isoform 2 (identifier: O70133-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     123-123: E → EA

Show »
Length:1,381
Mass (Da):149,546
Checksum:i0AB5502F91DEFB73
GO
Isoform 3 (identifier: O70133-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-216: Missing.

Show »
Length:1,164
Mass (Da):125,615
Checksum:iDA64E679A88D87C2
GO

Sequence cautioni

O70133: The sequence AAH89159 differs from that shown. Reason: Frameshift at positions 447 and 448.Curated
O70133: The sequence AAR87796 differs from that shown. Intron retention.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti46A → R in AAC05725 (PubMed:9480750).Curated1
Sequence conflicti136S → A in AAC05725 (PubMed:9480750).Curated1
Sequence conflicti136S → A in AAC05301 (PubMed:9480750).Curated1
Sequence conflicti187L → V (PubMed:14691545).Curated1
Sequence conflicti189Q → H in AAC05725 (PubMed:9480750).Curated1
Sequence conflicti211R → G in BAB28848 (PubMed:16141072).Curated1
Sequence conflicti235S → C in AAC05725 (PubMed:9480750).Curated1
Sequence conflicti257V → C in AAC05725 (PubMed:9480750).Curated1
Sequence conflicti281S → P in AAC05725 (PubMed:9480750).Curated1
Sequence conflicti674N → M in AAB72087 (Ref. 5) Curated1
Sequence conflicti748T → I in AAB72087 (Ref. 5) Curated1
Sequence conflicti831I → V in AAB72087 (Ref. 5) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0147781 – 216Missing in isoform 3. 1 PublicationAdd BLAST216
Alternative sequenceiVSP_014779123E → EA in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91922 mRNA. Translation: AAC05725.1.
AF023530 Genomic DNA. Translation: AAC05301.1.
AY512925 mRNA. Translation: AAR87796.1. Sequence problems.
BC089159 mRNA. Translation: AAH89159.1. Sequence problems.
AK013423 mRNA. Translation: BAB28848.1.
U92080 mRNA. Translation: AAB72087.1.
RefSeqiNP_031868.2. NM_007842.2.
UniGeneiMm.20000.

Genome annotation databases

GeneIDi13211.
KEGGimmu:13211.

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiDHX9_MOUSE
AccessioniPrimary (citable) accession number: O70133
Secondary accession number(s): O35931
, O54703, Q5FWY1, Q6R5F7, Q9CSA2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 19, 2005
Last modified: October 25, 2017
This is version 159 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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