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Q08211 (DHX9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent RNA helicase A

Short name=RHA
EC=3.6.4.13
Alternative name(s):
DEAH box protein 9
Leukophysin
Short name=LKP
Nuclear DNA helicase II
Short name=NDH II
Gene names
Name:DHX9
Synonyms:DDX9, LKP, NDH2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1270 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.23 Ref.24 Ref.28

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.30

Subunit structure

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). Ref.8 Ref.9 Ref.10 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.23 Ref.24 Ref.28 Ref.29

Subcellular location

Nucleusnucleolus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Can shuttle between nucleus and cytoplasm. Ref.2 Ref.13 Ref.20 Ref.24

Domain

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. Ref.11 Ref.12

Post-translational modification

Methylated. HRMT1L2 mediated methylation of undefined Arg residues in the NTD is required for nuclear localization. Ref.18

May be phosphorylated by PRKDC/XRCC7. Phosphorylated by EIF2AK2/PKR and this phosphorylation perturbs its association with dsRNA. Ref.17 Ref.23

Sequence similarities

Belongs to the DEAD box helicase family. DEAH subfamily.

Contains 2 DRBM (double-stranded RNA-binding) domains.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Biological processBiological rhythms
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandATP-binding
DNA-binding
Nucleotide-binding
RNA-binding
   Molecular functionActivator
Helicase
Hydrolase
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Traceable author statement Ref.3. Source: GOC

CRD-mediated mRNA stabilization

Inferred from mutant phenotype Ref.24. Source: UniProtKB

DNA duplex unwinding

Traceable author statement Ref.3. Source: GOC

RNA splicing

Traceable author statement. Source: Reactome

cellular response to heat

Inferred from electronic annotation. Source: Ensembl

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

osteoblast differentiation

Inferred from direct assay PubMed 16210410. Source: UniProt

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

   Cellular_componentCRD-mediated mRNA stability complex

Inferred from direct assay Ref.24. Source: UniProtKB

centrosome

Inferred from direct assay PubMed 17498979. Source: UniProtKB

cytoplasm

Traceable author statement Ref.2. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

membrane

Inferred from direct assay PubMed 16210410. Source: UniProt

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 17498979. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay Ref.20. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Traceable author statement Ref.3. Source: ProtInc

ATP-dependent RNA helicase activity

Traceable author statement Ref.3. Source: ProtInc

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA helicase activity

Traceable author statement Ref.2. Source: ProtInc

RNA polymerase II transcription factor binding

Inferred from physical interaction PubMed 17303075. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.20PubMed 17498979. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q08211-1)

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.
Isoform 2 (identifier: Q08211-2)

Also known as: Leukophysin; LKP;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12701270ATP-dependent RNA helicase A
PRO_0000055157

Regions

Domain3 – 7169DRBM 1
Domain180 – 25273DRBM 2
Domain398 – 564167Helicase ATP-binding
Domain636 – 809174Helicase C-terminal
Nucleotide binding411 – 4199ATP
Region1 – 250250Interaction with CREBBP
Region230 – 32596Interaction with BRCA1
Region331 – 38050MTAD
Region1151 – 1260110NTD
Motif511 – 5144DEIH box
Motif586 – 59510Nuclear localization signal Potential

Amino acid modifications

Modified residue871Phosphoserine Ref.22 Ref.26
Modified residue1461N6-acetyllysine By similarity
Modified residue1911N6-acetyllysine Ref.25
Modified residue1991N6-acetyllysine Ref.25
Modified residue3211Phosphoserine Ref.21
Modified residue10241N6-acetyllysine Ref.25

Natural variations

Alternative sequence1 – 10351035Missing in isoform 2.
VSP_042314
Natural variant8941I → V. Ref.1
Corresponds to variant rs1049264 [ dbSNP | Ensembl ].
VAR_052179

Experimental info

Mutagenesis3321W → A: Abrogates transcriptional activation by the MTAD domain. Ref.12
Mutagenesis3391W → A: Abrogates transcriptional activation and RNA polymerase II binding by the MTAD domain. Ref.12
Mutagenesis3421W → A: Abrogates transcriptional activation by the MTAD domain. Ref.12
Mutagenesis4171K → R: Abrogates transcriptional activation. Ref.9 Ref.16
Mutagenesis11631Missing: Abolishes nuclear localization. Ref.11
Mutagenesis11661R → L: Abolishes nuclear localization. Ref.11
Mutagenesis11661Missing: Abolishes nuclear localization. Ref.11
Sequence conflict201S → T in AAB48855. Ref.1
Sequence conflict108 – 1092TM → HH in AAB48855. Ref.1
Sequence conflict114 – 1163PPH → LHI in AAB48855. Ref.1
Sequence conflict1861N → I in AAB48855. Ref.1
Sequence conflict2601S → T in AAB48855. Ref.1
Sequence conflict4781I → V in AAB48855. Ref.1
Sequence conflict5211D → S in AAB48855. Ref.1
Sequence conflict5411L → F in AAB48855. Ref.1
Sequence conflict560 – 5656IIEVYG → SLKLW in AAB48855. Ref.1
Sequence conflict5901D → K in AAH25245. Ref.5
Sequence conflict7491A → S in AAB48855. Ref.1
Sequence conflict7491A → S in CAA71668. Ref.3
Sequence conflict768 – 7703VRP → STA in AAB48855. Ref.1
Sequence conflict768 – 7703VRP → STA in CAA71668. Ref.3
Sequence conflict8281A → G in AAI07882. Ref.5
Sequence conflict8991R → Q in AAB48855. Ref.1
Sequence conflict10371K → N in AAB48855. Ref.1
Sequence conflict10631T → P in AAB48855. Ref.1
Sequence conflict10631T → P in CAA71668. Ref.3
Sequence conflict11401R → E in AAB48855. Ref.1
Sequence conflict1204 – 12118NSFRAGYG → TPSGRIC in AAB48855. Ref.1
Sequence conflict1261 – 127010FGQGRGGGGY → LDIEEEVAAIKLGYVSSVCR Q in AAB48855. Ref.1

Secondary structure

............................................................... 1270
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 4.
Checksum: A607DA8F4C4B217A

FASTA1,270140,958
        10         20         30         40         50         60 
MGDVKNFLYA WCGKRKMTPS YEIRAVGNKN RQKFMCEVQV EGYNYTGMGN STNKKDAQSN 

        70         80         90        100        110        120 
AARDFVNYLV RINEIKSEEV PAFGVASPPP LTDTPDTTAN AEGDLPTTMG GPLPPHLALK 

       130        140        150        160        170        180 
AENNSEVGAS GYGVPGPTWD RGANLKDYYS RKEEQEVQAT LESEEVDLNA GLHGNWTLEN 

       190        200        210        220        230        240 
AKARLNQYFQ KEKIQGEYKY TQVGPDHNRS FIAEMTIYIK QLGRRIFARE HGSNKKLAAQ 

       250        260        270        280        290        300 
SCALSLVRQL YHLGVVEAYS GLTKKKEGET VEPYKVNLSQ DLEHQLQNII QELNLEILPP 

       310        320        330        340        350        360 
PEDPSVPVAL NIGKLAQFEP SQRQNQVGVV PWSPPQSNWN PWTSSNIDEG PLAFATPEQI 

       370        380        390        400        410        420 
SMDLKNELMY QLEQDHDLQA ILQERELLPV KKFESEILEA ISQNSVVIIR GATGCGKTTQ 

       430        440        450        460        470        480 
VPQFILDDFI QNDRAAECNI VVTQPRRISA VSVAERVAFE RGEEPGKSCG YSVRFESILP 

       490        500        510        520        530        540 
RPHASIMFCT VGVLLRKLEA GIRGISHVIV DEIHERDINT DFLLVVLRDV VQAYPEVRIV 

       550        560        570        580        590        600 
LMSATIDTSM FCEYFFNCPI IEVYGRTYPV QEYFLEDCIQ MTHFVPPPKD KKKKDKDDDG 

       610        620        630        640        650        660 
GEDDDANCNL ICGDEYGPET RLSMSQLNEK ETPFELIEAL LKYIETLNVP GAVLVFLPGW 

       670        680        690        700        710        720 
NLIYTMQKHL EMNPHFGSHR YQILPLHSQI PREEQRKVFD PVPVGVTKVI LSTNIAETSI 

       730        740        750        760        770        780 
TINDVVYVID SCKQKVKLFT AHNNMTNYAT VWASKTNLEQ RKGRAGRVRP GFCFHLCSRA 

       790        800        810        820        830        840 
RFERLETHMT PEMFRTPLHE IALSIKLLRL GGIGQFLAKA IEPPPLDAVI EAEHTLRELD 

       850        860        870        880        890        900 
ALDANDELTP LGRILAKLPI EPRFGKMMIM GCIFYVGDAI CTIAAATCFP EPFINEGKRL 

       910        920        930        940        950        960 
GYIHRNFAGN RFSDHVALLS VFQAWDDARM GGEEAEIRFC EHKRLNMATL RMTWEAKVQL 

       970        980        990       1000       1010       1020 
KEILINSGFP EDCLLTQVFT NTGPDNNLDV VISLLAFGVY PNVCYHKEKR KILTTEGRNA 

      1030       1040       1050       1060       1070       1080 
LIHKSSVNCP FSSQDMKYPS PFFVFGEKIR TRAISAKGMT LVTPLQLLLF ASKKVQSDGQ 

      1090       1100       1110       1120       1130       1140 
IVLVDDWIKL QISHEAAACI TGLRAAMEAL VVEVTKQPAI ISQLDPVNER MLNMIRQISR 

      1150       1160       1170       1180       1190       1200 
PSAAGINLMI GSTRYGDGPR PPKMARYDNG SGYRRGGSSY SGGGYGGGYS SGGYGSGGYG 

      1210       1220       1230       1240       1250       1260 
GSANSFRAGY GAGVGGGYRG VSRGGFRGNS GGDYRGPSGG YRGSGGFQRG GGRGAYGTGY 

      1270 
FGQGRGGGGY 

« Hide

Isoform 2 (Leukophysin) (LKP) [UniParc].

Checksum: B8A0D4E0C604A090
Show »

FASTA23524,336

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Dual roles of RNA helicase A in CREB-dependent transcription."
Aratani S., Fujii R., Oishi T., Fujita H., Amano T., Ohshima T., Hagiwara M., Fukamizu A., Nakajima T.
Mol. Cell. Biol. 21:4460-4469(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN MTAD, MUTAGENESIS OF TRP-332; TRP-339 AND TRP-342.
[13]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Antithetic effects of MBD2a on gene regulation."
Fujita H., Fujii R., Aratani S., Amano T., Fukamizu A., Nakajima T.
Mol. Cell. Biol. 23:2645-2657(2003) [PubMed] [Europe PMC] [Abstract]
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]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION.
[21]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[22]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS41444.1. [Q08211-1]
RefSeqNP_001348.2. NM_001357.4. [Q08211-1]
UniGeneHs.191518.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LLMX-ray2.80A/B329-563[»]
3VYXX-ray2.29A152-264[»]
3VYYX-ray2.90A/B1-91[»]
ProteinModelPortalQ08211.
SMRQ08211. Positions 1-86, 169-263, 329-1071.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108025. 195 interactions.
DIPDIP-31504N.
IntActQ08211. 53 interactions.
MINTMINT-5000572.
STRING9606.ENSP00000356520.

PTM databases

PhosphoSiteQ08211.

Polymorphism databases

DMDM116241330.

2D gel databases

SWISS-2DPAGEQ08211.

Proteomic databases

MaxQBQ08211.
PaxDbQ08211.
PRIDEQ08211.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367549; ENSP00000356520; ENSG00000135829. [Q08211-1]
GeneID1660.
KEGGhsa:1660.
UCSCuc001gpr.3. human. [Q08211-1]
uc009wyd.3. human. [Q08211-2]

Organism-specific databases

CTD1660.
GeneCardsGC01P182808.
H-InvDBHIX0001404.
HIX0149309.
HGNCHGNC:2750. DHX9.
HPACAB011819.
HPA028050.
HPA055684.
MIM603115. gene.
neXtProtNX_Q08211.
PharmGKBPA27232.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1643.
HOGENOMHOG000247063.
HOVERGENHBG039429.
InParanoidQ08211.
KOK13184.
OMAVDDWIRL.
OrthoDBEOG76471V.
PhylomeDBQ08211.
TreeFamTF313601.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

BgeeQ08211.
CleanExHS_DHX9.
GenevestigatorQ08211.

Family and domain databases

Gene3D3.30.160.20. 2 hits.
3.40.50.300. 2 hits.
InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
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]
PfamPF00270. DEAD. 1 hit.
PF00035. dsrm. 2 hits.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00358. DSRM. 2 hits.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00690. DEAH_ATP_HELICASE. 1 hit.
PS50137. DS_RBD. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRNA_Helicase_A.
GenomeRNAi1660.
NextBio6832.
PMAP-CutDBQ08211.
PROQ08211.
SOURCESearch...

Entry information

Entry nameDHX9_HUMAN
AccessionPrimary (citable) accession number: Q08211
Secondary accession number(s): B2RNV4 expand/collapse secondary AC list , Q05CI5, Q12803, Q32Q22, Q5VY62, Q6PD69, Q99556
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 159 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM