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Protein

ATP-dependent RNA helicase A

Gene

DHX9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Unwinds double-stranded DNA and RNA in a 3' to 5' direction. Alteration of secondary structure may subsequently influence interactions with proteins or other nucleic acids. Functions as a transcriptional activator. Component of the CRD-mediated complex that promotes MYC mRNA stability. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms. Positively regulates HIV-1 LTR-directed gene expression.3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi411 – 419ATP9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: ProtInc
  • ATP-dependent RNA helicase activity Source: ProtInc
  • DNA binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
  • RNA helicase activity Source: ProtInc
  • RNA polymerase II transcription factor binding Source: BHF-UCL

GO - Biological processi

  • CRD-mediated mRNA stabilization Source: UniProtKB
  • mRNA splicing, via spliceosome Source: Reactome
  • osteoblast differentiation Source: UniProtKB
  • positive regulation of type I interferon production Source: Reactome
  • protein localization to cytoplasmic stress granule Source: AgBase
  • rhythmic process Source: UniProtKB-KW
  • RNA processing Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Activator, Helicase, Hydrolase

Keywords - Biological processi

Biological rhythms

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000135829-MONOMER.
BRENDAi3.6.4.13. 2681.
ReactomeiR-HSA-1810476. RIP-mediated NFkB activation via ZBP1.
R-HSA-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-933542. TRAF6 mediated NF-kB activation.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase A (EC:3.6.4.13)
Short name:
RHA
Alternative name(s):
DEAH box protein 9
Leukophysin
Short name:
LKP
Nuclear DNA helicase II
Short name:
NDH II
Gene namesi
Name:DHX9
Synonyms:DDX9, LKP, NDH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:2750. DHX9.

Subcellular locationi

  • Nucleusnucleolus
  • Cytoplasm

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Can shuttle between nucleus and cytoplasm.

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • CRD-mediated mRNA stability complex Source: UniProtKB
  • cytoplasm Source: ProtInc
  • cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  • cytosol Source: Reactome
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • membrane Source: UniProtKB
  • nuclear stress granule Source: AgBase
  • nucleolus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi332W → A: Abrogates transcriptional activation by the MTAD domain. 1 Publication1
Mutagenesisi339W → A: Abrogates transcriptional activation and RNA polymerase II binding by the MTAD domain. 1 Publication1
Mutagenesisi342W → A: Abrogates transcriptional activation by the MTAD domain. 1 Publication1
Mutagenesisi417K → R: Abrogates transcriptional activation. 2 Publications1
Mutagenesisi1163Missing : Abolishes nuclear localization. 1 Publication1
Mutagenesisi1166R → L: Abolishes nuclear localization. 1 Publication1
Mutagenesisi1166Missing : Abolishes nuclear localization. 1 Publication1

Organism-specific databases

DisGeNETi1660.
OpenTargetsiENSG00000135829.
PharmGKBiPA27232.

Polymorphism and mutation databases

BioMutaiDHX9.
DMDMi116241330.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000551571 – 1270ATP-dependent RNA helicase AAdd BLAST1270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei87PhosphoserineCombined sources1
Modified residuei125PhosphoserineCombined sources1
Modified residuei146N6-acetyllysine; alternateBy similarity1
Modified residuei146N6-methyllysine; alternateCombined sources1
Modified residuei191N6-acetyllysineCombined sources1
Modified residuei199N6-acetyllysineCombined sources1
Modified residuei321PhosphoserineCombined sources1
Modified residuei449PhosphoserineCombined sources1
Modified residuei506PhosphoserineCombined sources1
Modified residuei1024N6-acetyllysineCombined sources1
Modified residuei1166Asymmetric dimethylarginineBy similarity1
Modified residuei1175Omega-N-methylarginineCombined sources1
Modified residuei1219Asymmetric dimethylarginineBy similarity1
Modified residuei1235Asymmetric dimethylarginineBy similarity1
Modified residuei1242Asymmetric dimethylarginineBy similarity1
Modified residuei1249Asymmetric dimethylarginineBy similarity1
Modified residuei1265Asymmetric dimethylarginineBy similarity1

Post-translational modificationi

Methylated. HRMT1L2 mediated methylation of undefined Arg residues in the NTD is required for nuclear localization.1 Publication
May be phosphorylated by PRKDC/XRCC7. Phosphorylated by EIF2AK2/PKR and this phosphorylation perturbs its association with dsRNA.2 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ08211.
MaxQBiQ08211.
PaxDbiQ08211.
PeptideAtlasiQ08211.
PRIDEiQ08211.
TopDownProteomicsiQ08211-1. [Q08211-1]

2D gel databases

SWISS-2DPAGEQ08211.

PTM databases

iPTMnetiQ08211.
PhosphoSitePlusiQ08211.
SwissPalmiQ08211.

Miscellaneous databases

PMAP-CutDBQ08211.

Expressioni

Gene expression databases

BgeeiENSG00000135829.
CleanExiHS_DHX9.
GenevisibleiQ08211. HS.

Organism-specific databases

HPAiCAB011819.
HPA028050.
HPA055684.

Interactioni

Subunit structurei

Interacts with ZIC2, IGF2BP1, IGF2BP2, IGF2BP3, MBD2, HRMT1L2/PRMT1, RELA and LARP6. Can also interact with XRCC5 and with TOP2A in an RNA dependent manner; these interactions may be indirect. Interaction with TOP2A is promoted by UBC9. Interacts with histone H2AFX and this requires phosphorylation of H2AFX on 'Ser-139'. Interacts (via N-terminus) with EIF2AK2/PKR and this interaction is dependent upon the activation of the kinase. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. May act to directly link BRCA1, CREBBP or SMN1 and the RNA polymerase II complex. 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. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active).14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF2AK2P195252EBI-352022,EBI-640775
NXF1Q9UBU98EBI-352022,EBI-398874
PRMT1Q998732EBI-352022,EBI-78738
RELAQ042064EBI-352022,EBI-73886
YBX1P6780910EBI-352022,EBI-354065
ZMAT3Q9HA383EBI-352022,EBI-2548480

GO - Molecular functioni

  • RNA polymerase II transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108025. 235 interactors.
DIPiDIP-31504N.
IntActiQ08211. 79 interactors.
MINTiMINT-5000572.
STRINGi9606.ENSP00000356520.

Structurei

Secondary structure

11270
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 14Combined sources11
Beta strandi20 – 28Combined sources9
Beta strandi31 – 39Combined sources9
Beta strandi47 – 53Combined sources7
Helixi54 – 71Combined sources18
Helixi77 – 79Combined sources3
Helixi170 – 173Combined sources4
Turni178 – 180Combined sources3
Helixi181 – 191Combined sources11
Beta strandi199 – 204Combined sources6
Helixi206 – 208Combined sources3
Beta strandi210 – 218Combined sources9
Helixi220 – 222Combined sources3
Beta strandi223 – 234Combined sources12
Helixi235 – 252Combined sources18
Turni341 – 344Combined sources4
Turni351 – 354Combined sources4
Helixi357 – 374Combined sources18
Helixi376 – 386Combined sources11
Helixi389 – 393Combined sources5
Helixi394 – 403Combined sources10
Beta strandi405 – 410Combined sources6
Helixi417 – 431Combined sources15
Helixi435 – 437Combined sources3
Beta strandi439 – 446Combined sources8
Helixi447 – 459Combined sources13
Turni460 – 462Combined sources3
Beta strandi467 – 473Combined sources7
Beta strandi476 – 478Combined sources3
Beta strandi482 – 490Combined sources9
Helixi491 – 500Combined sources10
Beta strandi507 – 510Combined sources4
Helixi518 – 533Combined sources16
Beta strandi537 – 543Combined sources7
Helixi549 – 554Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LLMX-ray2.80A/B329-563[»]
3VYXX-ray2.29A152-264[»]
3VYYX-ray2.90A/B1-91[»]
ProteinModelPortaliQ08211.
SMRiQ08211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 71DRBM 1PROSITE-ProRule annotationAdd BLAST69
Domaini180 – 252DRBM 2PROSITE-ProRule annotationAdd BLAST73
Domaini398 – 564Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST167
Domaini636 – 809Helicase C-terminalPROSITE-ProRule annotationAdd BLAST174

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 250Interaction with CREBBP1 PublicationAdd BLAST250
Regioni230 – 325Interaction with BRCA11 PublicationAdd BLAST96
Regioni331 – 380MTADAdd BLAST50
Regioni1151 – 1260NTDAdd BLAST110

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi511 – 514DEIH box4
Motifi586 – 595Nuclear localization signalSequence analysis10

Domaini

The MTAD domain mediates interaction with the RNA polymerase II holoenzyme. The NTD domain is necessary and sufficient for nucleo-cytoplasmic shuttling and interaction with HRMT1L2 and SMN1.2 Publications

Sequence similaritiesi

Contains 2 DRBM (double-stranded RNA-binding) domains.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0920. Eukaryota.
COG1643. LUCA.
GeneTreeiENSGT00760000119189.
HOGENOMiHOG000247063.
HOVERGENiHBG039429.
InParanoidiQ08211.
KOiK13184.
OMAiCSDHVAM.
OrthoDBiEOG091G0PKT.
PhylomeDBiQ08211.
TreeFamiTF313601.

Family and domain databases

Gene3Di3.30.160.20. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR011545. 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.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00035. dsrm. 2 hits.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00358. DSRM. 2 hits.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS50137. DS_RBD. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q08211-1) [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
MGDVKNFLYA WCGKRKMTPS YEIRAVGNKN RQKFMCEVQV EGYNYTGMGN
60 70 80 90 100
STNKKDAQSN AARDFVNYLV RINEIKSEEV PAFGVASPPP LTDTPDTTAN
110 120 130 140 150
AEGDLPTTMG GPLPPHLALK AENNSEVGAS GYGVPGPTWD RGANLKDYYS
160 170 180 190 200
RKEEQEVQAT LESEEVDLNA GLHGNWTLEN AKARLNQYFQ KEKIQGEYKY
210 220 230 240 250
TQVGPDHNRS FIAEMTIYIK QLGRRIFARE HGSNKKLAAQ SCALSLVRQL
260 270 280 290 300
YHLGVVEAYS GLTKKKEGET VEPYKVNLSQ DLEHQLQNII QELNLEILPP
310 320 330 340 350
PEDPSVPVAL NIGKLAQFEP SQRQNQVGVV PWSPPQSNWN PWTSSNIDEG
360 370 380 390 400
PLAFATPEQI SMDLKNELMY QLEQDHDLQA ILQERELLPV KKFESEILEA
410 420 430 440 450
ISQNSVVIIR GATGCGKTTQ VPQFILDDFI QNDRAAECNI VVTQPRRISA
460 470 480 490 500
VSVAERVAFE RGEEPGKSCG YSVRFESILP RPHASIMFCT VGVLLRKLEA
510 520 530 540 550
GIRGISHVIV DEIHERDINT DFLLVVLRDV VQAYPEVRIV LMSATIDTSM
560 570 580 590 600
FCEYFFNCPI IEVYGRTYPV QEYFLEDCIQ MTHFVPPPKD KKKKDKDDDG
610 620 630 640 650
GEDDDANCNL ICGDEYGPET RLSMSQLNEK ETPFELIEAL LKYIETLNVP
660 670 680 690 700
GAVLVFLPGW NLIYTMQKHL EMNPHFGSHR YQILPLHSQI PREEQRKVFD
710 720 730 740 750
PVPVGVTKVI LSTNIAETSI TINDVVYVID SCKQKVKLFT AHNNMTNYAT
760 770 780 790 800
VWASKTNLEQ RKGRAGRVRP GFCFHLCSRA RFERLETHMT PEMFRTPLHE
810 820 830 840 850
IALSIKLLRL GGIGQFLAKA IEPPPLDAVI EAEHTLRELD ALDANDELTP
860 870 880 890 900
LGRILAKLPI EPRFGKMMIM GCIFYVGDAI CTIAAATCFP EPFINEGKRL
910 920 930 940 950
GYIHRNFAGN RFSDHVALLS VFQAWDDARM GGEEAEIRFC EHKRLNMATL
960 970 980 990 1000
RMTWEAKVQL KEILINSGFP EDCLLTQVFT NTGPDNNLDV VISLLAFGVY
1010 1020 1030 1040 1050
PNVCYHKEKR KILTTEGRNA LIHKSSVNCP FSSQDMKYPS PFFVFGEKIR
1060 1070 1080 1090 1100
TRAISAKGMT LVTPLQLLLF ASKKVQSDGQ IVLVDDWIKL QISHEAAACI
1110 1120 1130 1140 1150
TGLRAAMEAL VVEVTKQPAI ISQLDPVNER MLNMIRQISR PSAAGINLMI
1160 1170 1180 1190 1200
GSTRYGDGPR PPKMARYDNG SGYRRGGSSY SGGGYGGGYS SGGYGSGGYG
1210 1220 1230 1240 1250
GSANSFRAGY GAGVGGGYRG VSRGGFRGNS GGDYRGPSGG YRGSGGFQRG
1260 1270
GGRGAYGTGY FGQGRGGGGY
Length:1,270
Mass (Da):140,958
Last modified:October 17, 2006 - v4
Checksum:iA607DA8F4C4B217A
GO
Isoform 2 (identifier: Q08211-2) [UniParc]FASTAAdd to basket
Also known as: Leukophysin, LKP

The sequence of this isoform differs from the canonical sequence as follows:
     1-1035: Missing.

Show »
Length:235
Mass (Da):24,336
Checksum:iB8A0D4E0C604A090
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti20S → T in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti108 – 109TM → HH in AAB48855 (PubMed:8344961).Curated2
Sequence conflicti114 – 116PPH → LHI in AAB48855 (PubMed:8344961).Curated3
Sequence conflicti186N → I in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti260S → T in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti478I → V in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti521D → S in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti541L → F in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti560 – 565IIEVYG → SLKLW in AAB48855 (PubMed:8344961).Curated6
Sequence conflicti590D → K in AAH25245 (PubMed:16710414).Curated1
Sequence conflicti749A → S in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti749A → S in CAA71668 (PubMed:9111062).Curated1
Sequence conflicti768 – 770VRP → STA in AAB48855 (PubMed:8344961).Curated3
Sequence conflicti768 – 770VRP → STA in CAA71668 (PubMed:9111062).Curated3
Sequence conflicti828A → G in AAI07882 (PubMed:16710414).Curated1
Sequence conflicti899R → Q in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti1037K → N in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti1063T → P in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti1063T → P in CAA71668 (PubMed:9111062).Curated1
Sequence conflicti1140R → E in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti1204 – 1211NSFRAGYG → TPSGRIC in AAB48855 (PubMed:8344961).Curated8
Sequence conflicti1261 – 1270FGQGRGGGGY → LDIEEEVAAIKLGYVSSVCR Q in AAB48855 (PubMed:8344961).Curated10

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052179894I → V.1 PublicationCorresponds to variant rs1049264dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0423141 – 1035Missing in isoform 2. 2 PublicationsAdd BLAST1035

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13848 mRNA. Translation: AAB48855.1.
U03643 mRNA. Translation: AAA03571.1.
Y10658 mRNA. Translation: CAA71668.1.
AB451248 mRNA. Translation: BAG70062.1.
AB451372 mRNA. Translation: BAG70186.1.
AL355999, AL662837 Genomic DNA. Translation: CAH71701.1.
AL662837, AL355999 Genomic DNA. Translation: CAI19277.1.
CH471067 Genomic DNA. Translation: EAW91138.1.
BC025245 mRNA. Translation: AAH25245.1.
BC058896 mRNA. Translation: AAH58896.1.
BC107881 mRNA. Translation: AAI07882.1.
BC137136 mRNA. Translation: AAI37137.1.
CCDSiCCDS41444.1. [Q08211-1]
RefSeqiNP_001348.2. NM_001357.4. [Q08211-1]
UniGeneiHs.191518.

Genome annotation databases

EnsembliENST00000367549; ENSP00000356520; ENSG00000135829. [Q08211-1]
GeneIDi1660.
KEGGihsa:1660.
UCSCiuc001gpr.4. human. [Q08211-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13848 mRNA. Translation: AAB48855.1.
U03643 mRNA. Translation: AAA03571.1.
Y10658 mRNA. Translation: CAA71668.1.
AB451248 mRNA. Translation: BAG70062.1.
AB451372 mRNA. Translation: BAG70186.1.
AL355999, AL662837 Genomic DNA. Translation: CAH71701.1.
AL662837, AL355999 Genomic DNA. Translation: CAI19277.1.
CH471067 Genomic DNA. Translation: EAW91138.1.
BC025245 mRNA. Translation: AAH25245.1.
BC058896 mRNA. Translation: AAH58896.1.
BC107881 mRNA. Translation: AAI07882.1.
BC137136 mRNA. Translation: AAI37137.1.
CCDSiCCDS41444.1. [Q08211-1]
RefSeqiNP_001348.2. NM_001357.4. [Q08211-1]
UniGeneiHs.191518.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LLMX-ray2.80A/B329-563[»]
3VYXX-ray2.29A152-264[»]
3VYYX-ray2.90A/B1-91[»]
ProteinModelPortaliQ08211.
SMRiQ08211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108025. 235 interactors.
DIPiDIP-31504N.
IntActiQ08211. 79 interactors.
MINTiMINT-5000572.
STRINGi9606.ENSP00000356520.

PTM databases

iPTMnetiQ08211.
PhosphoSitePlusiQ08211.
SwissPalmiQ08211.

Polymorphism and mutation databases

BioMutaiDHX9.
DMDMi116241330.

2D gel databases

SWISS-2DPAGEQ08211.

Proteomic databases

EPDiQ08211.
MaxQBiQ08211.
PaxDbiQ08211.
PeptideAtlasiQ08211.
PRIDEiQ08211.
TopDownProteomicsiQ08211-1. [Q08211-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367549; ENSP00000356520; ENSG00000135829. [Q08211-1]
GeneIDi1660.
KEGGihsa:1660.
UCSCiuc001gpr.4. human. [Q08211-1]

Organism-specific databases

CTDi1660.
DisGeNETi1660.
GeneCardsiDHX9.
H-InvDBHIX0001404.
HIX0149309.
HGNCiHGNC:2750. DHX9.
HPAiCAB011819.
HPA028050.
HPA055684.
MIMi603115. gene.
neXtProtiNX_Q08211.
OpenTargetsiENSG00000135829.
PharmGKBiPA27232.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0920. Eukaryota.
COG1643. LUCA.
GeneTreeiENSGT00760000119189.
HOGENOMiHOG000247063.
HOVERGENiHBG039429.
InParanoidiQ08211.
KOiK13184.
OMAiCSDHVAM.
OrthoDBiEOG091G0PKT.
PhylomeDBiQ08211.
TreeFamiTF313601.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000135829-MONOMER.
BRENDAi3.6.4.13. 2681.
ReactomeiR-HSA-1810476. RIP-mediated NFkB activation via ZBP1.
R-HSA-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-933542. TRAF6 mediated NF-kB activation.

Miscellaneous databases

ChiTaRSiDHX9. human.
GeneWikiiRNA_Helicase_A.
GenomeRNAii1660.
PMAP-CutDBQ08211.
PROiQ08211.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000135829.
CleanExiHS_DHX9.
GenevisibleiQ08211. HS.

Family and domain databases

Gene3Di3.30.160.20. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR011545. 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.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00035. dsrm. 2 hits.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00358. DSRM. 2 hits.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS50137. DS_RBD. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDHX9_HUMAN
AccessioniPrimary (citable) accession number: Q08211
Secondary accession number(s): B2RNV4
, Q05CI5, Q12803, Q32Q22, Q5VY62, Q6PD69, Q99556
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 186 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.