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P26196 (DDX6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable ATP-dependent RNA helicase DDX6

EC=3.6.4.13
Alternative name(s):
ATP-dependent RNA helicase p54
DEAD box protein 6
Oncogene RCK
Gene names
Name:DDX6
Synonyms:HLR2, RCK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In the process of mRNA degradation, may play a role in mRNA decapping.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Forms a complex with DCP1A, DCP2, EDC3 and EDC4/HEDLS. Interacts with LIMD1, WTIP and AJUBA. Interacts with APOBEC3G in an RNA-dependent manner. Interacts with RC3H1 By similarity. Ref.4 Ref.5 Ref.7 Ref.11

Subcellular location

CytoplasmP-body Ref.4 Ref.5 Ref.7 Ref.9.

Tissue specificity

Abundantly expressed in most tissues.

Involvement in disease

A chromosomal aberration involving DDX6 may be a cause of hematopoietic tumors such as B-cell lymphomas. Translocation t(11;14)(q23;q32).

Sequence similarities

Belongs to the DEAD box helicase family. DDX6/DHH1 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityChromosomal rearrangement
   DiseaseProto-oncogene
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

cytoplasmic mRNA processing body assembly

Inferred from direct assay PubMed 20826699. Source: MGI

exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Traceable author statement. Source: Reactome

   Cellular_componentRISC complex

Inferred from direct assay Ref.7. Source: MGI

cytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic mRNA processing body

Inferred from direct assay Ref.5Ref.9. Source: UniProtKB

cytoplasmic stress granule

Inferred from direct assay PubMed 17392519. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

RNA helicase activity

Traceable author statement Ref.1. Source: ProtInc

helicase activity

Traceable author statement Ref.3Ref.1. Source: ProtInc

poly(A) RNA binding

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

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483Probable ATP-dependent RNA helicase DDX6
PRO_0000054983

Regions

Domain127 – 298172Helicase ATP-binding
Domain308 – 468161Helicase C-terminal
Nucleotide binding140 – 1478ATP By similarity
Motif96 – 12429Q motif
Motif246 – 2494DEAD box

Amino acid modifications

Modified residue361Phosphothreonine Ref.6

Experimental info

Mutagenesis3201Q → A: Abolishes interaction with EDC3; when associated with A-323; A-327 and A-331. Ref.11
Mutagenesis3231H → A: Abolishes interaction with EDC3; when associated with A-320; A-327 and A-331. Ref.11
Mutagenesis3271T → A: Abolishes interaction with EDC3; when associated with A-320; A-323 and A-331. Ref.11
Mutagenesis3311R → A: Abolishes interaction with EDC3; when associated with A-320; A-323 and A-327. Ref.11
Sequence conflict2931Q → E in Z11685. Ref.1

Secondary structure

...................................................................... 483
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26196 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: F802C642861793FB

FASTA48354,417
        10         20         30         40         50         60 
MSTARTENPV IMGLSSQNGQ LRGPVKPTGG PGGGGTQTQQ QMNQLKNTNT INNGTQQQAQ 

        70         80         90        100        110        120 
SMTTTIKPGD DWKKTLKLPP KDLRIKTSDV TSTKGNEFED YCLKRELLMG IFEMGWEKPS 

       130        140        150        160        170        180 
PIQEESIPIA LSGRDILARA KNGTGKSGAY LIPLLERLDL KKDNIQAMVI VPTRELALQV 

       190        200        210        220        230        240 
SQICIQVSKH MGGAKVMATT GGTNLRDDIM RLDDTVHVVI ATPGRILDLI KKGVAKVDHV 

       250        260        270        280        290        300 
QMIVLDEADK LLSQDFVQIM EDIILTLPKN RQILLYSATF PLSVQKFMNS HLQKPYEINL 

       310        320        330        340        350        360 
MEELTLKGVT QYYAYVTERQ KVHCLNTLFS RLQINQSIIF CNSSQRVELL AKKISQLGYS 

       370        380        390        400        410        420 
CFYIHAKMRQ EHRNRVFHDF RNGLCRNLVC TDLFTRGIDI QAVNVVINFD FPKLAETYLH 

       430        440        450        460        470        480 
RIGRSGRFGH LGLAINLITY DDRFNLKSIE EQLGTEIKPI PSNIDKSLYV AEYHSEPVED 


EKP 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, expression and localization of an RNA helicase gene from a human lymphoid cell line with chromosomal breakpoint 11q23.3."
Lu D., Yunis J.J.
Nucleic Acids Res. 20:1967-1972(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: Skin.
[3]"The RCK gene associated with t(11;14) translocation is distinct from the MLL/ALL-1 gene with t(4;11) and t(11;19) translocations."
Akao Y., Seto M., Yamamoto K., Iida S., Nakazawa S., Inazawa J., Abe T., Takahashi T., Ueda R.
Cancer Res. 52:6083-6087(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-483.
Tissue: Lung.
[4]"Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping."
Fenger-Groen M., Fillman C., Norrild B., Lykke-Andersen J.
Mol. Cell 20:905-915(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DCP1A; DCP2; EDC3 AND EDC4, SUBCELLULAR LOCATION.
[5]"Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies."
Wichroski M.J., Robb G.B., Rana T.M.
PLoS Pathog. 2:E41-E41(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH APOBEC3G.
[6]"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 THR-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[7]"LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-mediated gene silencing."
James V., Zhang Y., Foxler D.E., de Moor C.H., Kong Y.W., Webb T.M., Self T.J., Feng Y., Lagos D., Chu C.Y., Rana T.M., Morley S.J., Longmore G.D., Bushell M., Sharp T.V.
Proc. Natl. Acad. Sci. U.S.A. 107:12499-12504(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LIMD1; WTIP AND AJUBA.
[8]"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].
[9]"HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies."
Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.
J. Virol. 86:11712-11724(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Crystallization and X-ray analysis of the N-terminal core domain of a tumour-associated human DEAD-box RNA helicase, rck/p54."
Matsui T., Hogetsu K., Akao Y., Tanaka M., Sato T., Kumasaka T., Tanaka N.
Acta Crystallogr. D 60:156-159(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 94-299.
[11]"Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B."
Tritschler F., Braun J.E., Eulalio A., Truffault V., Izaurralde E., Weichenrieder O.
Mol. Cell 33:661-668(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 296-483 IN COMPLEX WITH EDC3, MUTAGENESIS OF GLN-320; HIS-323; THR-327 AND ARG-331, INTERACTION WITH EDC3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11685 mRNA. No translation available.
BC065007 mRNA. Translation: AAH65007.1.
D17532 mRNA. Translation: BAA04482.1.
PIRS22651.
RefSeqNP_001244120.1. NM_001257191.2.
NP_004388.2. NM_004397.5.
XP_005271474.1. XM_005271417.2.
UniGeneHs.408461.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VECX-ray2.01A/B94-299[»]
2WAXX-ray2.30A/C296-483[»]
2WAYX-ray2.30A/C296-483[»]
ProteinModelPortalP26196.
SMRP26196. Positions 63-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108022. 38 interactions.
DIPDIP-29195N.
IntActP26196. 31 interactions.
MINTMINT-5004149.
STRING9606.ENSP00000264018.

PTM databases

PhosphoSiteP26196.

Polymorphism databases

DMDM116241327.

2D gel databases

DOSAC-COBS-2DPAGEP26196.

Proteomic databases

PaxDbP26196.
PeptideAtlasP26196.
PRIDEP26196.

Protocols and materials databases

DNASU1656.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264018; ENSP00000264018; ENSG00000110367.
ENST00000526070; ENSP00000433704; ENSG00000110367.
ENST00000534980; ENSP00000442266; ENSG00000110367.
ENST00000593895; ENSP00000472890; ENSG00000269612.
ENST00000596625; ENSP00000471023; ENSG00000269612.
ENST00000600727; ENSP00000469200; ENSG00000269612.
GeneID1656.
KEGGhsa:1656.
UCSCuc001pub.2. human.

Organism-specific databases

CTD1656.
GeneCardsGC11M118619.
HGNCHGNC:2747. DDX6.
HPACAB004668.
HPA024201.
HPA026644.
MIM600326. gene.
neXtProtNX_P26196.
PharmGKBPA27229.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0513.
HOGENOMHOG000268797.
HOVERGENHBG106685.
InParanoidP26196.
KOK12614.
OMAEEFCLKR.
OrthoDBEOG7D85W7.
PhylomeDBP26196.
TreeFamTF300440.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP26196.
BgeeP26196.
CleanExHS_DDX6.
GenevestigatorP26196.

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.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[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

ChiTaRSDDX6. human.
EvolutionaryTraceP26196.
GeneWikiDDX6.
GenomeRNAi1656.
NextBio6820.
PROP26196.
SOURCESearch...

Entry information

Entry nameDDX6_HUMAN
AccessionPrimary (citable) accession number: P26196
Secondary accession number(s): Q5D048
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 151 of the entry and version 2 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 chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM