Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q08211

- DHX9_HUMAN

UniProt

Q08211 - DHX9_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

ATP-dependent RNA helicase A

Gene

DHX9

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi411 – 4199ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent DNA helicase activity Source: ProtInc
  3. ATP-dependent RNA helicase activity Source: ProtInc
  4. DNA binding Source: UniProtKB-KW
  5. poly(A) RNA binding Source: UniProtKB
  6. RNA helicase activity Source: ProtInc
  7. RNA polymerase II transcription factor binding Source: BHF-UCL

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. cellular response to heat Source: Ensembl
  3. circadian rhythm Source: Ensembl
  4. CRD-mediated mRNA stabilization Source: UniProtKB
  5. DNA duplex unwinding Source: GOC
  6. gene expression Source: Reactome
  7. innate immune response Source: Reactome
  8. mRNA splicing, via spliceosome Source: Reactome
  9. osteoblast differentiation Source: UniProt
  10. positive regulation of type I interferon production Source: Reactome
  11. RNA splicing Source: Reactome
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

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_467. mRNA Splicing - Major Pathway.

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
ProteomesiUP000005640: 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

  1. centrosome Source: UniProtKB
  2. CRD-mediated mRNA stability complex Source: UniProtKB
  3. cytoplasm Source: ProtInc
  4. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  5. cytosol Source: Reactome
  6. membrane Source: UniProtKB
  7. nucleolus Source: HPA
  8. nucleoplasm Source: Reactome
  9. nucleus Source: UniProtKB
  10. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi332 – 3321W → A: Abrogates transcriptional activation by the MTAD domain. 1 Publication
Mutagenesisi339 – 3391W → A: Abrogates transcriptional activation and RNA polymerase II binding by the MTAD domain. 1 Publication
Mutagenesisi342 – 3421W → A: Abrogates transcriptional activation by the MTAD domain. 1 Publication
Mutagenesisi417 – 4171K → R: Abrogates transcriptional activation. 2 Publications
Mutagenesisi1163 – 11631Missing: Abolishes nuclear localization. 1 Publication
Mutagenesisi1166 – 11661R → L: Abolishes nuclear localization. 1 Publication
Mutagenesisi1166 – 11661Missing: Abolishes nuclear localization. 1 Publication

Organism-specific databases

PharmGKBiPA27232.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12701270ATP-dependent RNA helicase APRO_0000055157Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871Phosphoserine2 Publications
Modified residuei146 – 1461N6-acetyllysineBy similarity
Modified residuei191 – 1911N6-acetyllysine1 Publication
Modified residuei199 – 1991N6-acetyllysine1 Publication
Modified residuei321 – 3211Phosphoserine1 Publication
Modified residuei1024 – 10241N6-acetyllysine1 Publication

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.5 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ08211.
PaxDbiQ08211.
PRIDEiQ08211.

2D gel databases

SWISS-2DPAGEQ08211.

PTM databases

PhosphoSiteiQ08211.

Miscellaneous databases

PMAP-CutDBQ08211.

Expressioni

Gene expression databases

BgeeiQ08211.
CleanExiHS_DHX9.
GenevestigatoriQ08211.

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

Protein-protein interaction databases

BioGridi108025. 203 interactions.
DIPiDIP-31504N.
IntActiQ08211. 54 interactions.
MINTiMINT-5000572.
STRINGi9606.ENSP00000356520.

Structurei

Secondary structure

1
1270
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1411Combined sources
Beta strandi20 – 289Combined sources
Beta strandi31 – 399Combined sources
Beta strandi47 – 537Combined sources
Helixi54 – 7118Combined sources
Helixi77 – 793Combined sources
Helixi170 – 1734Combined sources
Turni178 – 1803Combined sources
Helixi181 – 19111Combined sources
Beta strandi199 – 2046Combined sources
Helixi206 – 2083Combined sources
Beta strandi210 – 2189Combined sources
Helixi220 – 2223Combined sources
Beta strandi223 – 23412Combined sources
Helixi235 – 25218Combined sources
Turni341 – 3444Combined sources
Turni351 – 3544Combined sources
Helixi357 – 37418Combined sources
Helixi376 – 38611Combined sources
Helixi389 – 3935Combined sources
Helixi394 – 40310Combined sources
Beta strandi405 – 4106Combined sources
Helixi417 – 43115Combined sources
Helixi435 – 4373Combined sources
Beta strandi439 – 4468Combined sources
Helixi447 – 45913Combined sources
Turni460 – 4623Combined sources
Beta strandi467 – 4737Combined sources
Beta strandi476 – 4783Combined sources
Beta strandi482 – 4909Combined sources
Helixi491 – 50010Combined sources
Beta strandi507 – 5104Combined sources
Helixi518 – 53316Combined sources
Beta strandi537 – 5437Combined sources
Helixi549 – 5546Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LLMX-ray2.80A/B329-563[»]
3VYXX-ray2.29A152-264[»]
3VYYX-ray2.90A/B1-91[»]
ProteinModelPortaliQ08211.
SMRiQ08211. Positions 1-86, 169-263, 329-1071.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 7169DRBM 1PROSITE-ProRule annotationAdd
BLAST
Domaini180 – 25273DRBM 2PROSITE-ProRule annotationAdd
BLAST
Domaini398 – 564167Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini636 – 809174Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 250250Interaction with CREBBPAdd
BLAST
Regioni230 – 32596Interaction with BRCA1Add
BLAST
Regioni331 – 38050MTADAdd
BLAST
Regioni1151 – 1260110NTDAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi511 – 5144DEIH box
Motifi586 – 59510Nuclear localization signalSequence Analysis

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

eggNOGiCOG1643.
GeneTreeiENSGT00760000119189.
HOGENOMiHOG000247063.
HOVERGENiHBG039429.
InParanoidiQ08211.
KOiK13184.
OMAiVDDWIRL.
OrthoDBiEOG76471V.
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. dsRNA-bd_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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201S → T in AAB48855. (PubMed:8344961)Curated
Sequence conflicti108 – 1092TM → HH in AAB48855. (PubMed:8344961)Curated
Sequence conflicti114 – 1163PPH → LHI in AAB48855. (PubMed:8344961)Curated
Sequence conflicti186 – 1861N → I in AAB48855. (PubMed:8344961)Curated
Sequence conflicti260 – 2601S → T in AAB48855. (PubMed:8344961)Curated
Sequence conflicti478 – 4781I → V in AAB48855. (PubMed:8344961)Curated
Sequence conflicti521 – 5211D → S in AAB48855. (PubMed:8344961)Curated
Sequence conflicti541 – 5411L → F in AAB48855. (PubMed:8344961)Curated
Sequence conflicti560 – 5656IIEVYG → SLKLW in AAB48855. (PubMed:8344961)Curated
Sequence conflicti590 – 5901D → K in AAH25245. (PubMed:16710414)Curated
Sequence conflicti749 – 7491A → S in AAB48855. (PubMed:8344961)Curated
Sequence conflicti749 – 7491A → S in CAA71668. (PubMed:9111062)Curated
Sequence conflicti768 – 7703VRP → STA in AAB48855. (PubMed:8344961)Curated
Sequence conflicti768 – 7703VRP → STA in CAA71668. (PubMed:9111062)Curated
Sequence conflicti828 – 8281A → G in AAI07882. (PubMed:16710414)Curated
Sequence conflicti899 – 8991R → Q in AAB48855. (PubMed:8344961)Curated
Sequence conflicti1037 – 10371K → N in AAB48855. (PubMed:8344961)Curated
Sequence conflicti1063 – 10631T → P in AAB48855. (PubMed:8344961)Curated
Sequence conflicti1063 – 10631T → P in CAA71668. (PubMed:9111062)Curated
Sequence conflicti1140 – 11401R → E in AAB48855. (PubMed:8344961)Curated
Sequence conflicti1204 – 12118NSFRAGYG → TPSGRIC in AAB48855. (PubMed:8344961)Curated
Sequence conflicti1261 – 127010FGQGRGGGGY → LDIEEEVAAIKLGYVSSVCR Q in AAB48855. (PubMed:8344961)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti894 – 8941I → V.1 Publication
Corresponds to variant rs1049264 [ dbSNP | Ensembl ].
VAR_052179

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 10351035Missing in isoform 2. 2 PublicationsVSP_042314Add
BLAST

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.3. human. [Q08211-1]
uc009wyd.3. human. [Q08211-2]

Polymorphism databases

DMDMi116241330.

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 .
CCDSi CCDS41444.1. [Q08211-1 ]
RefSeqi NP_001348.2. NM_001357.4. [Q08211-1 ]
UniGenei Hs.191518.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LLM X-ray 2.80 A/B 329-563 [» ]
3VYX X-ray 2.29 A 152-264 [» ]
3VYY X-ray 2.90 A/B 1-91 [» ]
ProteinModelPortali Q08211.
SMRi Q08211. Positions 1-86, 169-263, 329-1071.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108025. 203 interactions.
DIPi DIP-31504N.
IntActi Q08211. 54 interactions.
MINTi MINT-5000572.
STRINGi 9606.ENSP00000356520.

PTM databases

PhosphoSitei Q08211.

Polymorphism databases

DMDMi 116241330.

2D gel databases

SWISS-2DPAGE Q08211.

Proteomic databases

MaxQBi Q08211.
PaxDbi Q08211.
PRIDEi Q08211.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367549 ; ENSP00000356520 ; ENSG00000135829 . [Q08211-1 ]
GeneIDi 1660.
KEGGi hsa:1660.
UCSCi uc001gpr.3. human. [Q08211-1 ]
uc009wyd.3. human. [Q08211-2 ]

Organism-specific databases

CTDi 1660.
GeneCardsi GC01P182808.
H-InvDB HIX0001404.
HIX0149309.
HGNCi HGNC:2750. DHX9.
HPAi CAB011819.
HPA028050.
HPA055684.
MIMi 603115. gene.
neXtProti NX_Q08211.
PharmGKBi PA27232.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1643.
GeneTreei ENSGT00760000119189.
HOGENOMi HOG000247063.
HOVERGENi HBG039429.
InParanoidi Q08211.
KOi K13184.
OMAi VDDWIRL.
OrthoDBi EOG76471V.
PhylomeDBi Q08211.
TreeFami TF313601.

Enzyme and pathway databases

Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi DHX9. human.
GeneWikii RNA_Helicase_A.
GenomeRNAii 1660.
NextBioi 6832.
PMAP-CutDB Q08211.
PROi Q08211.
SOURCEi Search...

Gene expression databases

Bgeei Q08211.
CleanExi HS_DHX9.
Genevestigatori Q08211.

Family and domain databases

Gene3Di 3.30.160.20. 2 hits.
3.40.50.300. 2 hits.
InterProi IPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR014720. dsRNA-bd_dom.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00270. DEAD. 1 hit.
PF00035. dsrm. 2 hits.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00358. DSRM. 2 hits.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS00690. DEAH_ATP_HELICASE. 1 hit.
PS50137. DS_RBD. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human RNA helicase A is homologous to the maleless protein of Drosophila."
    Lee C.-G., Hurwitz J.
    J. Biol. Chem. 268:16822-16830(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT VAL-894.
  2. "Leukophysin: an RNA helicase A-related molecule identified in cytotoxic T cell granules and vesicles."
    Abdelhaleem M.M., Hameed S., Klassen D., Greenberg A.H.
    J. Immunol. 156:2026-2035(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION.
  3. "Domain structure of human nuclear DNA helicase II (RNA helicase A)."
    Zhang S., Grosse F.
    J. Biol. Chem. 272:11487-11494(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain, Muscle and Uterus.
  8. "A functional interaction between the survival motor neuron complex and RNA polymerase II."
    Pellizzoni L., Charroux B., Rappsilber J., Mann M., Dreyfuss G.
    J. Cell Biol. 152:75-85(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH SMN1, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "RNA helicase A mediates association of CBP with RNA polymerase II."
    Nakajima T., Uchida C., Anderson S.F., Lee C.-G., Hurwitz J., Parvin J.D., Montminy M.
    Cell 90:1107-1112(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CREBBP AND RNA POLYMERASE II, MUTAGENESIS OF LYS-417.
  10. "BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A."
    Anderson S.F., Schlegel B.P., Nakajima T., Wolpin E.S., Parvin J.D.
    Nat. Genet. 19:254-256(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRCA1.
  11. "The carboxyl terminus of RNA helicase A contains a bidirectional nuclear transport domain."
    Tang H., McDonald D., Middlesworth T., Hope T.J., Wong-Staal F.
    Mol. Cell. Biol. 19:3540-3550(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN NTD, MUTAGENESIS OF LYS-1163 AND ARG-1166.
  12. Cited for: DOMAIN MTAD, MUTAGENESIS OF TRP-332; TRP-339 AND TRP-342.
  13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: INTERACTION WITH MBD2.
  15. "RNA helicase A interacts with dsDNA and topoisomerase IIalpha."
    Zhou K., Choe K.-T., Zaidi Z., Wang Q., Mathews M.B., Lee C.-G.
    Nucleic Acids Res. 31:2253-2260(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOP2A.
  16. "RNA helicase A interacts with nuclear factor kappaB p65 and functions as a transcriptional coactivator."
    Tetsuka T., Uranishi H., Sanda T., Asamitsu K., Yang J.-P., Wong-Staal F., Okamoto T.
    Eur. J. Biochem. 271:3741-3751(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RELA, MUTAGENESIS OF LYS-417.
  17. "DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent manner."
    Zhang S., Schlott B., Goerlach M., Grosse F.
    Nucleic Acids Res. 32:1-10(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH XRCC5, PHOSPHORYLATION BY PRKDC.
  18. "Arginine methylation of RNA helicase a determines its subcellular localization."
    Smith W.A., Schurter B.T., Wong-Staal F., David M.
    J. Biol. Chem. 279:22795-22798(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION.
  19. "Actinomycin D induces histone gamma-H2AX foci and complex formation of gamma-H2AX with Ku70 and nuclear DNA helicase II."
    Mischo H.E., Hemmerich P., Grosse F., Zhang S.
    J. Biol. Chem. 280:9586-9594(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH H2AFX.
  20. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "An antiviral response directed by PKR phosphorylation of the RNA helicase A."
    Sadler A.J., Latchoumanin O., Hawkes D., Mak J., Williams B.R.
    PLoS Pathog. 5:E1000311-E1000311(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EIF2AK2, PHOSPHORYLATION.
  24. "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
    Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
    RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  25. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191; LYS-199 AND LYS-1024, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "A novel role of RNA helicase A in regulation of translation of type I collagen mRNAs."
    Manojlovic Z., Stefanovic B.
    RNA 18:321-334(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN COLLAGEN MRNA STABILIZATION, INTERACTION WITH LARP6.
  29. "Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding proteins) is modulated by distinct RNA-binding domains."
    Wachter K., Kohn M., Stohr N., Huttelmaier S.
    Biol. Chem. 394:1077-1090(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3.
  30. "Crystal structure of human RNA helicase A (DHX9): structural basis for unselective nucleotide base binding in a DEAD-box variant protein."
    Schutz P., Wahlberg E., Karlberg T., Hammarstrom M., Collins R., Flores A., Schuler H.
    J. Mol. Biol. 400:768-782(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 329-563 IN COMPLEX WITH ADP, NUCLEOTIDE-BINDING, CATALYTIC ACTIVITY.

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 26, 2014
This is version 163 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

External Data

Dasty 3