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Q61656 (DDX5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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 RNA helicase DEAD1
Short name=mDEAD1
DEAD box protein 5
RNA helicase p68
Gene names
Name:Ddx5
Synonyms:Tnz2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Ref.3 Ref.4

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 By similarity. Interacts with BRDT. Ref.5

Subcellular location

Nucleusnucleolus By similarity.

Post-translational modification

Sumoylated; sumoylation, promoted by PIAS1, promotes interaction with HDAC1 and transcriptional repression activity. Sumoylation also significantly increases stability, and reduces polyubiquitination By similarity.

Polyubiquitinated, leading to proteasomal degradation By similarity.

Sequence similarities

Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Caution

Silenced gene expression via RNA interference in Ref.3 and Ref.4 was simultaneously performed with DDX5 and DDX17; siRNA-resistant DDX5 expression was able to rescue the effect in muscle differentiation.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentNucleus
Spliceosome
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

circadian rhythm

Inferred from mutant phenotype PubMed 22767893. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 17435748. Source: MGI

intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15464984. Source: MGI

regulation of alternative mRNA splicing, via spliceosome

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of androgen receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of osteoblast differentiation

Inferred from mutant phenotype Ref.4. Source: UniProtKB

regulation of skeletal muscle cell differentiation

Inferred from mutant phenotype Ref.3. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred by curator PubMed 15464984. Source: MGI

ribonucleoprotein complex

Inferred from sequence orthology PubMed 18809582. Source: MGI

spliceosomal complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA helicase activity

Inferred from sequence or structural similarity. Source: UniProtKB

androgen receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

estrogen receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription cofactor activity

Inferred from direct assay PubMed 15464984. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 614614Probable ATP-dependent RNA helicase DDX5
PRO_0000054992

Regions

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

Sites

Binding site1211ATP By similarity

Amino acid modifications

Modified residue321N6-acetyllysine By similarity
Modified residue331N6-acetyllysine By similarity
Modified residue401N6-acetyllysine Ref.6
Modified residue2361N6-acetyllysine Ref.6
Modified residue2971Phosphotyrosine By similarity
Modified residue4801Phosphoserine By similarity
Modified residue5021Omega-N-methylated arginine By similarity
Cross-link53Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Experimental info

Sequence conflict1121Q → H in CAA46581. Ref.1
Sequence conflict1591Q → H in CAA46581. Ref.1
Sequence conflict5971L → V in CAA46581. Ref.1
Sequence conflict6001A → P in CAA46581. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61656 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: A9BBB25D9B7B8819

FASTA61469,290
        10         20         30         40         50         60 
MSSYSSDRDR GRDRGFGAPR FGGSRTGPLS GKKFGNPGEK LVKKKWNLDE LPKFEKNFYQ 

        70         80         90        100        110        120 
EHPDLARRTA QEVDTYRRSK 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 RENYDRGYSN LLKRDFGAKT QNGVYSAANY 

       550        560        570        580        590        600 
TNGSFGSNFV SAGIQTSFRT GNPTGTYQNG YDSTQQYGSN VANMHNGMNQ QAYAYPLPQA 

       610 
APMIGYPMPT GYSQ 

« Hide

References

« Hide 'large scale' references
[1]"High-level expression in male germ cells of murine P68 RNA helicase mRNA."
Lemaire L., Heinlein U.A.O.
Life Sci. 52:917-926(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Testis.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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.
[4]"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.
[5]"The testis-specific double bromodomain-containing protein BRDT forms a complex with multiple spliceosome components and is required for mRNA splicing and 3'-UTR truncation in round spermatids."
Berkovits B.D., Wang L., Guarnieri P., Wolgemuth D.J.
Nucleic Acids Res. 40:7162-7175(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRDT.
[6]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40 AND LYS-236, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65627 mRNA. Translation: CAA46581.1.
AL603664 Genomic DNA. No translation available.
PIRI48385.
UniGeneMm.491096.

3D structure databases

ProteinModelPortalQ61656.
SMRQ61656. Positions 52-473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-32293N.
IntActQ61656. 9 interactions.
MINTMINT-1549637.

PTM databases

PhosphoSiteQ61656.

Proteomic databases

PaxDbQ61656.
PRIDEQ61656.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCuc007lzs.1. mouse.

Organism-specific databases

MGIMGI:105037. Ddx5.

Phylogenomic databases

eggNOGCOG0513.
HOVERGENHBG015893.
InParanoidQ61656.

Gene expression databases

CleanExMM_DDX5.
GenevestigatorQ61656.

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. mouse.
PROQ61656.
SOURCESearch...

Entry information

Entry nameDDX5_MOUSE
AccessionPrimary (citable) accession number: Q61656
Secondary accession number(s): E9Q105
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot