P17844 (DDX5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable ATP-dependent RNA helicase DDX5
EC=3.6.4.13

Alternative name(s):
DEAD box protein 5
RNA helicase p68

Gene names

Name:	DDX5
Synonyms:	G17P1, HELR, HLR1

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	614 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for estrogen receptor ESR1 and androgen receptor AR. Increases ESR1 AF-1 domain-mediated transactivation and ESR1 AF-1 and AF-2 domains transcriptional synergistic activity. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specicic manner; the function probbaly involves association with histone deacetylases, such as HDAC1. Ref.10 Ref.12 Ref.15 Ref.16 Ref.17 Ref.19 Ref.22 Ref.23 Ref.25 Ref.30
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Interacts with BRDT By similarity. Identified in the spliceosome C complex. Interacts with RBM4; the interaction occurs in a RNA-independent manner. Interacts with EIF2C1 and EIF2C2. Interacts with ESR1; the interaction is enhanced by phosphorylation of ESR1 AF-1 domain. Interacts with AR, NCOA1, NCOA2, NCOA3, EP300, CREBBP, POLR2A, TP53, RUNX2 and HDAC1. Self-associates. Interacts with DDX17. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.30
Subcellular location	Nucleus › nucleolus Ref.2 Ref.11.
Post-translational modification	Arg-502 is dimethylated, probably to asymmetric dimethylarginine. Sumoylated; sumoylation, promoted by PIAS1, promotes interaction with HDAC1 and transcriptional repression activity. Sumoylation also significantly increases stability, and reduces polyubiquitination. Ref.21 Ref.27 Polyubiquitinated, leading to proteasomal degradation.
Sequence similarities	Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell growth Non-traceable author statement Ref.8. Source: UniProtKB circadian rhythm Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara intrinsic apoptotic signaling pathway by p53 class mediator Inferred from mutant phenotype Ref.17. Source: UniProtKB mRNA splicing, via spliceosome Inferred by curator Ref.13. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.16. Source: UniProtKB positive regulation of DNA damage response, signal transduction by p53 class mediator Inferred from mutant phenotype Ref.17. Source: UniProtKB positive regulation of intracellular estrogen receptor signaling pathway Inferred from direct assay Ref.10Ref.12. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.10. Source: UniProtKB regulation of alternative mRNA splicing, via spliceosome Inferred from direct assay Ref.30. Source: UniProtKB regulation of androgen receptor signaling pathway Inferred from mutant phenotype Ref.22. Source: UniProtKB regulation of osteoblast differentiation Inferred from sequence or structural similarity. Source: UniProtKB regulation of skeletal muscle cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB regulation of viral genome replication Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	catalytic step 2 spliceosome Inferred from direct assay Ref.13. Source: UniProtKB nucleolus Inferred from direct assay Ref.11. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent RNA helicase activity Inferred from electronic annotation. Source: Compara RNA helicase activity Inferred from mutant phenotype Ref.30. Source: UniProtKB androgen receptor binding Inferred from direct assay Ref.22. Source: UniProtKB estrogen receptor binding Inferred from direct assay Ref.10. Source: UniProtKB pre-mRNA binding Inferred from direct assay Ref.30. Source: UniProtKB transcription coactivator activity Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CHD3	Q12873	4	EBI-351962,EBI-523590
Crebbp	P45481	3	EBI-351962,EBI-296306	From a different organism.
EP300	Q09472	4	EBI-351962,EBI-447295
ESR1	P03372	8	EBI-351962,EBI-78473
FBL	P22087	6	EBI-351962,EBI-358318
HDAC1	Q13547	4	EBI-351962,EBI-301834
MBD3	O95983	4	EBI-351962,EBI-1783068
Myod1	P10085	3	EBI-351962,EBI-4405734	From a different organism.
NFAT5	O94916	4	EBI-351962,EBI-308320
POLR2A	P24928	3	EBI-351962,EBI-295301
Runx2	Q08775-3	2	EBI-351962,EBI-6119991	From a different organism.
TP53	P04637	3	EBI-351962,EBI-366083
TP53	P04637-1	2	EBI-351962,EBI-3895849
TP53	P04637-7	2	EBI-351962,EBI-3895873

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 614

614

Probable ATP-dependent RNA helicase DDX5

PRO_0000054991

Regions

Domain

125 – 300

176

Helicase ATP-binding

Domain

328 – 475

148

Helicase C-terminal

Nucleotide binding

114 – 116

3

ATP

Nucleotide binding

138 – 145

8

ATP

Region

477 – 614

138

Transactivation domain

Motif

94 – 122

29

Q motif

Motif

248 – 251

4

DEAD box

Sites

Binding site

121

1

ATP

Amino acid modifications

Modified residue

32

1

N6-acetyllysine Ref.26

Modified residue

33

1

N6-acetyllysine Ref.26

Modified residue

40

1

N6-acetyllysine Ref.26

Modified residue

297

1

Phosphotyrosine Ref.18

Modified residue

480

1

Phosphoserine Ref.28 Ref.31

Cross-link

53

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.21 Ref.27

Natural variations

Natural variant

480

1

S → A.
Corresponds to variant rs1140409 [ dbSNP | Ensembl ].

VAR_029241

Experimental info

Mutagenesis

53

1

K → R: Abolishes sumoylation, abolishes interaction with HDAC1, increases TP53 coactivation and promotes polyubiquitination. Ref.21 Ref.27

Mutagenesis

55

1

E → A: Abolishes sumoylation. Ref.21

Mutagenesis

144

1

K → R: Abolishes RNA helicase activity, no effect on transcriptional coactivator function. Ref.10 Ref.19

Mutagenesis

403

1

R → L: Binds to the tau stem-loop-containing RNA. Inhibits tau exon 10 inclusion and RNA cleavage. Does not inhibit interaction with RBM4. Ref.30

Secondary structure

1

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614

Helix Strand Turn

Details...

Helix

64 – 66

3

Helix

72 – 80

9

Beta strand

82 – 87

6

Turn

96 – 99

4

Helix

103 – 110

8

Turn

111 – 113

3

Helix

119 – 130

12

Beta strand

134 – 138

5

Helix

144 – 157

14

Beta strand

169 – 173

5

Helix

177 – 193

17

Beta strand

198 – 201

4

Helix

207 – 216

10

Beta strand

219 – 223

5

Helix

225 – 233

9

Turn

234 – 236

3

Beta strand

239 – 241

3

Beta strand

244 – 247

4

Helix

250 – 255

6

Helix

259 – 266

8

Beta strand

274 – 280

7

Helix

284 – 293

10

Beta strand

298 – 302

5

Sequences

	Sequence		Length	Mass (Da)
	P17844 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 84DF684FD6871594	FASTA	614	69,148
	10 20 30 40 50 60 MSGYSSDRDR GRDRGFGAPR FGGSRAGPLS GKKFGNPGEK LVKKKWNLDE LPKFEKNFYQ 70 80 90 100 110 120 EHPDLARRTA QEVETYRRSK EITVRGHNCP KPVLNFYEAN FPANVMDVIA RQNFTEPTAI 130 140 150 160 170 180 QAQGWPVALS GLDMVGVAQT GSGKTLSYLL PAIVHINHQP FLERGDGPIC LVLAPTRELA 190 200 210 220 230 240 QQVQQVAAEY CRACRLKSTC IYGGAPKGPQ IRDLERGVEI CIATPGRLID FLECGKTNLR 250 260 270 280 290 300 RTTYLVLDEA DRMLDMGFEP QIRKIVDQIR PDRQTLMWSA TWPKEVRQLA EDFLKDYIHI 310 320 330 340 350 360 NIGALELSAN HNILQIVDVC HDVEKDEKLI RLMEEIMSEK ENKTIVFVET KRRCDELTRK 370 380 390 400 410 420 MRRDGWPAMG IHGDKSQQER DWVLNEFKHG KAPILIATDV ASRGLDVEDV KFVINYDYPN 430 440 450 460 470 480 SSEDYIHRIG RTARSTKTGT AYTFFTPNNI KQVSDLISVL REANQAINPK LLQLVEDRGS 490 500 510 520 530 540 GRSRGRGGMK DDRRDRYSAG KRGGFNTFRD RENYDRGYSS LLKRDFGAKT QNGVYSAANY 550 560 570 580 590 600 TNGSFGSNFV SAGIQTSFRT GNPTGTYQNG YDSTQQYGSN VPNMHNGMNQ QAYAYPATAA 610 APMIGYPMPT GYSQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete cDNA sequence of the human p68 protein." Hloch P., Stahl H. Nucleic Acids Res. 18:3045-3045(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"p68 RNA helicase: identification of a nucleolar form and cloning of related genes containing a conserved intron in yeasts." Iggo R.D., Jamieson D.J., McNeill S.A., Southgate J., McPheat J., Lane D.P. Mol. Cell. Biol. 11:1326-1333(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
[3]	"Structure and expression of the human p68 RNA helicase gene." Roessler O.G., Hloch P., Schutz N., Weitzenegger T., Stahl H. Nucleic Acids Res. 28:932-939(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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].
[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 (SEP-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]. Tissue: Muscle.
[8]	"Nuclear protein with sequence homology to translation initiation factor eIF-4A." Ford M.J., Anton I.A., Lane D.P. Nature 332:736-738(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-614.
[9]	"Molecular organization of the murine p68 RNA helicase gene promotor region." Petry P., Bammer S., Heinlein U.A.O. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-163.
[10]	"Purification and identification of p68 RNA helicase acting as a transcriptional coactivator specific for the activation function 1 of human estrogen receptor alpha." Endoh H., Maruyama K., Masuhiro Y., Kobayashi Y., Goto M., Tai H., Yanagisawa J., Metzger D., Hashimoto S., Kato S. Mol. Cell. Biol. 19:5363-5372(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH ESR1, MUTAGENESIS OF LYS-144.
[11]	"The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase." Nicol S.M., Causevic M., Prescott A.R., Fuller-Pace F.V. Exp. Cell Res. 257:272-280(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FBL, SUBCELLULAR LOCATION.
[12]	"A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor alpha coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA." Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S., Arao Y., Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y., Kato S. EMBO J. 20:1341-1352(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH ESR1; NCOA1; NCOA2 AND NCOA3.
[13]	"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis." Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J. RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[14]	"The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells." Ogilvie V.C., Wilson B.J., Nicol S.M., Morrice N.A., Saunders L.R., Barber G.N., Fuller-Pace F.V. Nucleic Acids Res. 31:1470-1480(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SELF-ASSOCIATION, INTERACTION WITH DDX17.
[15]	"Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300." Rossow K.L., Janknecht R. Oncogene 22:151-156(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH EP300; CREBBP AND POLR2A.
[16]	"The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner." Wilson B.J., Bates G.J., Nicol S.M., Gregory D.J., Perkins N.D., Fuller-Pace F.V. BMC Mol. Biol. 5:11-11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TRANSCRIPTIONAL REPRESSION, INTERACTION WITH HDAC1.
[17]	"The DEAD box protein p68: a novel transcriptional coactivator of the p53 tumour suppressor." Bates G.J., Nicol S.M., Wilson B.J., Jacobs A.M., Bourdon J.C., Wardrop J., Gregory D.J., Lane D.P., Perkins N.D., Fuller-Pace F.V. EMBO J. 24:543-553(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH TP53.
[18]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-297, MASS SPECTROMETRY.
[19]	"The RNA helicases p68/p72 and the noncoding RNA SRA are coregulators of MyoD and skeletal muscle differentiation." Caretti G., Schiltz R.L., Dilworth F.J., Di Padova M., Zhao P., Ogryzko V., Fuller-Pace F.V., Hoffman E.P., Tapscott S.J., Sartorelli V. Dev. Cell 11:547-560(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MYOD1, MUTAGENESIS OF LYS-144.
[20]	"Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells." Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G. EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF2C1 AND EIF2C2.
[21]	"SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1." Jacobs A.M., Nicol S.M., Hislop R.G., Jaffray E.G., Hay R.T., Fuller-Pace F.V. Oncogene 26:5866-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-53, INTERACTION WITH HDAC1 AND PIAS1, MUTAGENESIS OF LYS-53 AND GLU-55.
[22]	"The RNA helicase p68 is a novel androgen receptor coactivator involved in splicing and is overexpressed in prostate cancer." Clark E.L., Coulson A., Dalgliesh C., Rajan P., Nicol S.M., Fleming S., Heer R., Gaughan L., Leung H.Y., Elliott D.J., Fuller-Pace F.V., Robson C.N. Cancer Res. 68:7938-7946(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH AR.
[23]	"p68 (Ddx5) interacts with Runx2 and regulates osteoblast differentiation." Jensen E.D., Niu L., Caretti G., Nicol S.M., Teplyuk N., Stein G.S., Sartorelli V., van Wijnen A.J., Fuller-Pace F.V., Westendorf J.J. J. Cell. Biochem. 103:1438-1451(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RUNX2.
[24]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[25]	"The DEAD-box protein p72 regulates ERalpha-/oestrogen-dependent transcription and cell growth, and is associated with improved survival in ERalpha-positive breast cancer." Wortham N.C., Ahamed E., Nicol S.M., Thomas R.S., Periyasamy M., Jiang J., Ochocka A.M., Shousha S., Huson L., Bray S.E., Coombes R.C., Ali S., Fuller-Pace F.V. Oncogene 28:4053-4064(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ESR1.
[26]	"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-32; LYS-33 AND LYS-40, MASS SPECTROMETRY.
[27]	"Sumoylation of p68 and p72 RNA helicases affects protein stability and transactivation potential." Mooney S.M., Grande J.P., Salisbury J.L., Janknecht R. Biochemistry 49:1-10(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-53, MUTAGENESIS OF LYS-53, POLYUBIQUITINATION.
[28]	"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-480, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"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].
[30]	"RNA helicase p68 (DDX5) regulates tau exon 10 splicing by modulating a stem-loop structure at the 5' splice site." Kar A., Fushimi K., Zhou X., Ray P., Shi C., Chen X., Liu Z., Chen S., Wu J.Y. Mol. Cell. Biol. 31:1812-1821(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RBM4, MUTAGENESIS OF ARG-403, RNA-BINDING.
[31]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, MASS SPECTROMETRY.
[32]	"Comparative structural analysis of human DEAD-box RNA helicases." Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L., Hogbom M., Holmberg-Schiavone L., Tempel W., Park H.W., Hammarstrom M., Moche M., Thorsell A.G., Schuler H. PLoS ONE 5:E12791-E12791(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 68-307 IN COMPLEX WITH ADP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X52104 mRNA. Translation: CAA36324.1.
AF015812 Genomic DNA. Translation: AAB84094.1.
BT006943 mRNA. Translation: AAP35589.1.
AB451257 mRNA. Translation: BAG70071.1.
CH471109 Genomic DNA. Translation: EAW94202.1.
CH471109 Genomic DNA. Translation: EAW94203.1.
BC016027 mRNA. Translation: AAH16027.1.
X15729 mRNA. Translation: CAA33751.1.
AJ010931 Genomic DNA. Translation: CAA09408.1.

IPI

IPI00017617.

PIR

JC1087.

RefSeq

NP_004387.1. NM_004396.3.

UniGene

Hs.279806.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FE2	X-ray	2.60	A/B	68-307	[»]
4A4D	X-ray	2.70	A	52-304	[»]

ProteinModelPortal

P17844.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29844N.

IntAct

P17844. 53 interactions.

MINT

MINT-5000516.

STRING

9606.ENSP00000225792.

PTM databases

PhosphoSite

P17844.

Polymorphism databases

DMDM

129383.

2D gel databases

SWISS-2DPAGE

P17844.

Proteomic databases

PaxDb

P17844.

PeptideAtlas

P17844.

PRIDE

P17844.

Protocols and materials databases

DNASU

1655.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000225792; ENSP00000225792; ENSG00000108654.
ENST00000574715; ENSP00000459637; ENSG00000263077.

GeneID

1655.

KEGG

hsa:1655.

UCSC

uc002jej.2. human.

Organism-specific databases

CTD

1655.

GeneCards

GC17M062494.

HGNC

HGNC:2746. DDX5.

HPA

CAB005868.
HPA020043.

MIM

180630. gene.

neXtProt

NX_P17844.

PharmGKB

PA27228.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0513.

HOGENOM

HOG000268804.

HOVERGEN

HBG015893.

InParanoid

P17844.

KO

K12823.

OMA

IDAMSGY.

OrthoDB

EOG4BVRTM.

PhylomeDB

P17844.

Gene expression databases

ArrayExpress

P17844.

Bgee

P17844.

CleanEx

HS_DDX5.

Genevestigator

P17844.

GermOnline

ENSG00000108654. Homo sapiens.

Family and domain databases

InterPro

IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR012587. P68HR.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]

Pfam

PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF08061. P68HR. 2 hits.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

PROSITE

PS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DDX5. human.

EvolutionaryTrace

P17844.

GenomeRNAi

1655.

NextBio

6816.

SOURCE

Search...

Entry information

Entry name

DDX5_HUMAN

Accession

Primary (citable) accession number: P17844
Secondary accession number(s): B5BU21 , D3DU32, O75681, Q53Y61

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 1, 2013
This is version 153 of the entry and version 1 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.