Q08211 (DHX9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1270 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.23 Ref.27
Catalytic activity	ATP + H2O = ADP + phosphate. Ref.28
Subunit structure	Interacts with ZIC2 By similarity. 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 mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with IGF2BP1. Binds MBD2, HRMT1L2/PRMT1, and RELA. May act to directly link BRCA1, CREBBP or SMN1 and the RNA polymerase II complex. 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 with LARP6. Ref.8 Ref.9 Ref.10 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.23 Ref.27
Subcellular location	Nucleus › nucleolus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Can shuttle between nucleus and cytoplasm. Ref.2 Ref.13 Ref.20 Ref.23
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. Ref.17
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
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	ATP-binding DNA-binding Nucleotide-binding RNA-binding
Molecular function	Activator Helicase Hydrolase
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	CRD-mediated mRNA stabilization Inferred from mutant phenotype Ref.23. Source: UniProtKB cellular response to heat Inferred from electronic annotation. Source: Compara circadian rhythm Inferred from electronic annotation. Source: Compara mRNA splicing, via spliceosome Traceable author statement. Source: Reactome
Cellular_component	CRD-mediated mRNA stability complex Inferred from direct assay Ref.23. Source: UniProtKB centrosome Inferred from direct assay PubMed 17498979. Source: UniProtKB nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome ribonucleoprotein complex Inferred from direct assay Ref.20. Source: UniProtKB
Molecular_function	ATP 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 double-stranded RNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF2AK2	P19525	2	EBI-352022,EBI-640775
NXF1	Q9UBU9	8	EBI-352022,EBI-398874
PRMT1	Q99873	2	EBI-352022,EBI-78738
RELA	Q04206	4	EBI-352022,EBI-73886

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1270

1270

ATP-dependent RNA helicase A

PRO_0000055157

Regions

Domain

3 – 71

69

DRBM 1

Domain

180 – 252

73

DRBM 2

Domain

398 – 564

167

Helicase ATP-binding

Domain

636 – 809

174

Helicase C-terminal

Nucleotide binding

411 – 419

9

ATP

Region

1 – 250

250

Interaction with CREBBP

Region

230 – 325

96

Interaction with BRCA1

Region

331 – 380

50

MTAD

Region

1151 – 1260

110

NTD

Motif

511 – 514

4

DEIH box

Motif

586 – 595

10

Nuclear localization signal Potential

Amino acid modifications

Modified residue

87

1

Phosphoserine Ref.22 Ref.25

Modified residue

191

1

N6-acetyllysine Ref.24

Modified residue

199

1

N6-acetyllysine Ref.24

Modified residue

321

1

Phosphoserine Ref.21

Modified residue

1024

1

N6-acetyllysine Ref.24

Natural variations

Alternative sequence

1 – 1035

1035

Missing in isoform 2.

VSP_042314

Natural variant

894

1

I → V. Ref.1
Corresponds to variant rs1049264 [ dbSNP | Ensembl ].

VAR_052179

Experimental info

Mutagenesis

332

1

W → A: Abrogates transcriptional activation by the MTAD domain. Ref.12

Mutagenesis

339

1

W → A: Abrogates transcriptional activation and RNA polymerase II binding by the MTAD domain. Ref.12

Mutagenesis

342

1

W → A: Abrogates transcriptional activation by the MTAD domain. Ref.12

Mutagenesis

417

1

K → R: Abrogates transcriptional activation. Ref.9 Ref.16

Mutagenesis

1163

1

Missing: Abolishes nuclear localization. Ref.11

Mutagenesis

1166

1

R → L: Abolishes nuclear localization. Ref.11

Mutagenesis

1166

1

Missing: Abolishes nuclear localization. Ref.11

Sequence conflict

20

1

S → T in AAB48855. Ref.1

Sequence conflict

108 – 109

2

TM → HH in AAB48855. Ref.1

Sequence conflict

114 – 116

3

PPH → LHI in AAB48855. Ref.1

Sequence conflict

186

1

N → I in AAB48855. Ref.1

Sequence conflict

260

1

S → T in AAB48855. Ref.1

Sequence conflict

478

1

I → V in AAB48855. Ref.1

Sequence conflict

521

1

D → S in AAB48855. Ref.1

Sequence conflict

541

1

L → F in AAB48855. Ref.1

Sequence conflict

560 – 565

6

IIEVYG → SLKLW in AAB48855. Ref.1

Sequence conflict

590

1

D → K in AAH25245. Ref.5

Sequence conflict

749

1

A → S in AAB48855. Ref.1

Sequence conflict

749

1

A → S in CAA71668. Ref.3

Sequence conflict

768 – 770

3

VRP → STA in AAB48855. Ref.1

Sequence conflict

768 – 770

3

VRP → STA in CAA71668. Ref.3

Sequence conflict

828

1

A → G in AAI07882. Ref.5

Sequence conflict

899

1

R → Q in AAB48855. Ref.1

Sequence conflict

1037

1

K → N in AAB48855. Ref.1

Sequence conflict

1063

1

T → P in AAB48855. Ref.1

Sequence conflict

1063

1

T → P in CAA71668. Ref.3

Sequence conflict

1140

1

R → E in AAB48855. Ref.1

Sequence conflict

1204 – 1211

8

NSFRAGYG → TPSGRIC in AAB48855. Ref.1

Sequence conflict

1261 – 1270

10

FGQGRGGGGY → LDIEEEVAAIKLGYVSSVCR Q in AAB48855. Ref.1

Secondary structure

1

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1270

Helix Strand Turn

Details...

Helix

4 – 14

11

Beta strand

20 – 28

9

Beta strand

31 – 39

9

Beta strand

47 – 53

7

Helix

54 – 71

18

Helix

77 – 79

3

Helix

170 – 173

4

Turn

178 – 180

3

Helix

181 – 191

11

Beta strand

199 – 204

6

Helix

206 – 208

3

Beta strand

210 – 218

9

Helix

220 – 222

3

Beta strand

223 – 234

12

Helix

235 – 252

18

Turn

341 – 344

4

Turn

351 – 354

4

Helix

357 – 374

18

Helix

376 – 386

11

Helix

389 – 393

5

Helix

394 – 403

10

Beta strand

405 – 410

6

Helix

417 – 431

15

Helix

435 – 437

3

Beta strand

439 – 446

8

Helix

447 – 459

13

Turn

460 – 462

3

Beta strand

467 – 473

7

Beta strand

476 – 478

3

Beta strand

482 – 490

9

Helix

491 – 500

10

Beta strand

507 – 510

4

Helix

518 – 533

16

Beta strand

537 – 543

7

Helix

549 – 554

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 4. Checksum: A607DA8F4C4B217A	FASTA	1,270	140,958
	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
	Isoform 2 (Leukophysin) (LKP) [UniParc]. Checksum: B8A0D4E0C604A090	FASTA	235	24,336
	10 20 30 40 50 60 MKYPSPFFVF GEKIRTRAIS AKGMTLVTPL QLLLFASKKV QSDGQIVLVD DWIKLQISHE 70 80 90 100 110 120 AAACITGLRA AMEALVVEVT KQPAIISQLD PVNERMLNMI RQISRPSAAG INLMIGSTRY 130 140 150 160 170 180 GDGPRPPKMA RYDNGSGYRR GGSSYSGGGY GGGYSSGGYG SGGYGGSANS FRAGYGAGVG 190 200 210 220 230 GGYRGVSRGG FRGNSGGDYR GPSGGYRGSG GFQRGGGRGA YGTGYFGQGR GGGGY

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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: IDENTIFICATION BY MASS SPECTROMETRY, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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.
[24]	"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, MASS SPECTROMETRY.
[25]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"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].
[27]	"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.
[28]	"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.

IPI

IPI00844578.

RefSeq

NP_001348.2. NM_001357.4.

UniGene

Hs.191518.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q08211.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31504N.

IntAct

Q08211. 29 interactions.

MINT

MINT-5000572.

STRING

9606.ENSP00000356520.

PTM databases

PhosphoSite

Q08211.

Polymorphism databases

DMDM

116241330.

2D gel databases

SWISS-2DPAGE

Q08211.

Proteomic databases

PaxDb

Q08211.

PRIDE

Q08211.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367549; ENSP00000356520; ENSG00000135829.

GeneID

1660.

KEGG

hsa:1660.

UCSC

uc001gpr.3. human.

Organism-specific databases

CTD

1660.

GeneCards

GC01P182808.

H-InvDB

HIX0001404.
HIX0149309.

HGNC

HGNC:2750. DHX9.

HPA

CAB011819.
HPA028050.

MIM

603115. gene.

neXtProt

NX_Q08211.

PharmGKB

PA27232.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1643.

HOGENOM

HOG000247063.

HOVERGEN

HBG039429.

InParanoid

Q08211.

KO

K13184.

OMA

DDWIRLQ.

OrthoDB

EOG4HHP1J.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

Bgee

Q08211.

CleanEx

HS_DHX9.

Genevestigator

Q08211.

GermOnline

ENSG00000135829. Homo sapiens.

Family and domain databases

Gene3D

3.30.160.20. 2 hits.

InterPro

IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR001159. Ds-RNA-bd.
IPR014720. dsRNA-bd-like_dom.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
[Graphical view]

Pfam

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]

SMART

SM00487. DEXDc. 1 hit.
SM00358. DSRM. 2 hits.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

PROSITE

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]

ProtoNet

Search...

Other

GenomeRNAi

1660.

NextBio

6832.

PMAP-CutDB

Q08211.

SOURCE

Search...

Entry information

Entry name

DHX9_HUMAN

Accession

Primary (citable) accession number: Q08211
Secondary accession number(s): B2RNV4 , Q05CI5, Q12803, Q32Q22, Q5VY62, Q6PD69, Q99556

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 145 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.