Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P17844 (DDX5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 166. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length614 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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. 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

Identified in the spliceosome C complex. Interacts with RBM4; the interaction occurs in an RNA-independent manner. Interacts with AGO1 and AGO2. 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. Interacts with BRDT. 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.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

Nucleusnucleolus 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 processBiological rhythms
mRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentNucleus
Spliceosome
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell growth

Non-traceable author statement Ref.8. Source: UniProtKB

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.13. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleolus

Inferred from direct assay Ref.11. Source: UniProtKB

nucleus

Non-traceable author statement Ref.8. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay PubMed 18809582. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent RNA helicase activity

Inferred from electronic annotation. Source: Ensembl

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

poly(A) RNA binding

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

pre-mRNA binding

Inferred from direct assay Ref.30. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.20Ref.30. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 614614Probable ATP-dependent RNA helicase DDX5
PRO_0000054991

Regions

Domain125 – 300176Helicase ATP-binding
Domain328 – 475148Helicase C-terminal
Nucleotide binding114 – 1163ATP
Nucleotide binding138 – 1458ATP
Region477 – 614138Transactivation domain
Motif94 – 12229Q motif
Motif248 – 2514DEAD box

Sites

Binding site1211ATP

Amino acid modifications

Modified residue321N6-acetyllysine Ref.26
Modified residue331N6-acetyllysine Ref.26
Modified residue401N6-acetyllysine Ref.26
Modified residue2361N6-acetyllysine By similarity
Modified residue2971Phosphotyrosine Ref.18
Modified residue4801Phosphoserine Ref.28 Ref.31
Cross-link53Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.21 Ref.27

Natural variations

Natural variant4801S → A.
Corresponds to variant rs1140409 [ dbSNP | Ensembl ].
VAR_029241

Experimental info

Mutagenesis531K → R: Abolishes sumoylation, abolishes interaction with HDAC1, increases TP53 coactivation and promotes polyubiquitination. Ref.21 Ref.27
Mutagenesis551E → A: Abolishes sumoylation. Ref.21
Mutagenesis1441K → R: Abolishes RNA helicase activity, no effect on transcriptional coactivator function. Ref.10 Ref.19
Mutagenesis4031R → 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

............................................. 614
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17844 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 84DF684FD6871594

FASTA61469,148
        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 

« Hide

References

« Hide '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. 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].
[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 (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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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 AGO1 AND AGO2.
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
CCDSCCDS11659.1.
PIRJC1087.
RefSeqNP_004387.1. NM_004396.3.
XP_005257168.1. XM_005257111.1.
XP_006721801.1. XM_006721738.1.
UniGeneHs.279806.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FE2X-ray2.60A/B68-307[»]
4A4DX-ray2.70A52-304[»]
ProteinModelPortalP17844.
SMRP17844. Positions 50-473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108021. 164 interactions.
DIPDIP-29844N.
IntActP17844. 81 interactions.
MINTMINT-5000516.
STRING9606.ENSP00000225792.

PTM databases

PhosphoSiteP17844.

Polymorphism databases

DMDM129383.

2D gel databases

SWISS-2DPAGEP17844.

Proteomic databases

MaxQBP17844.
PaxDbP17844.
PeptideAtlasP17844.
PRIDEP17844.

Protocols and materials databases

DNASU1655.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225792; ENSP00000225792; ENSG00000108654.
ENST00000574715; ENSP00000459637; ENSG00000263077.
GeneID1655.
KEGGhsa:1655.
UCSCuc002jej.2. human.

Organism-specific databases

CTD1655.
GeneCardsGC17M062494.
HGNCHGNC:2746. DDX5.
HPACAB005868.
HPA020043.
MIM180630. gene.
neXtProtNX_P17844.
PharmGKBPA27228.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0513.
HOGENOMHOG000268804.
HOVERGENHBG015893.
InParanoidP17844.
KOK12823.
PhylomeDBP17844.
TreeFamTF300332.

Gene expression databases

ArrayExpressP17844.
BgeeP17844.
CleanExHS_DDX5.
GenevestigatorP17844.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR012587. P68HR.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF08061. P68HR. 2 hits.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDDX5. human.
EvolutionaryTraceP17844.
GeneWikiDDX5.
GenomeRNAi1655.
NextBio6816.
PROP17844.
SOURCESearch...

Entry information

Entry nameDDX5_HUMAN
AccessionPrimary (citable) accession number: P17844
Secondary accession number(s): B5BU21 expand/collapse secondary AC list , D3DU32, O75681, Q53Y61
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: July 9, 2014
This is version 166 of the entry and version 1 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 17

Human chromosome 17: entries, gene names and cross-references to MIM