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HUMAN:DDX6

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) DDX6 (synonyms: HLR2, RCK)
Protein Name(s) Probable ATP-dependent RNA helicase DDX6

ATP-dependent RNA helicase p54 DEAD box protein 6 Oncogene RCK

External Links
UniProt P26196
EMBL Z11685
BC065007
D17532
CCDS CCDS44751.1
PIR S22651
RefSeq NP_001244120.1
NP_004388.2
XP_005271474.1
UniGene Hs.408461
PDB 1VEC
2WAX
2WAY
4CRW
4CT4
4CT5
PDBsum 1VEC
2WAX
2WAY
4CRW
4CT4
4CT5
ProteinModelPortal P26196
SMR P26196
BioGrid 108022
DIP DIP-29195N
IntAct P26196
MINT MINT-5004149
STRING 9606.ENSP00000264018
PhosphoSite P26196
DMDM 116241327
DOSAC-COBS-2DPAGE P26196
MaxQB P26196
PaxDb P26196
PeptideAtlas P26196
PRIDE P26196
DNASU 1656
Ensembl ENST00000526070
ENST00000534980
ENST00000620157
GeneID 1656
KEGG hsa:1656
UCSC uc001pub.2
CTD 1656
GeneCards GC11M118619
HGNC HGNC:2747
HPA CAB004668
HPA024201
HPA026644
MIM 600326
neXtProt NX_P26196
PharmGKB PA27229
eggNOG COG0513
GeneTree ENSGT00740000115573
HOGENOM HOG000268797
HOVERGEN HBG106685
InParanoid P26196
KO K12614
OMA RIYQKVQ
OrthoDB EOG7D85W7
PhylomeDB P26196
TreeFam TF300440
Reactome REACT_20518
ChiTaRS DDX6
EvolutionaryTrace P26196
GeneWiki DDX6
GenomeRNAi 1656
NextBio 6820
PRO PR:P26196
Proteomes UP000005640
Bgee P26196
CleanEx HS_DDX6
ExpressionAtlas P26196
Genevestigator P26196
GO GO:0005737
GO:0000932
GO:0010494
GO:0005829
GO:0043231
GO:0016020
GO:0016442
GO:0005524
GO:0008026
GO:0004386
GO:0044822
GO:0003724
GO:0033962
GO:0043928
GO:0010467
GO:0016071
GO:0000288
GO:0016070
Gene3D 3.40.50.300
InterPro IPR011545
IPR014001
IPR001650
IPR027417
IPR000629
IPR014014
Pfam PF00270
PF00271
SMART SM00487
SM00490
SUPFAM SSF52540
PROSITE PS00039
PS51192
PS51194
PS51195

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0000932

cytoplasmic mRNA processing body

PMID:22022269[1]

IMP: Inferred from Mutant Phenotype

C

Fig. 2AB

complete
CACAO 2728

GO:0019074

viral RNA genome packaging

PMID:22022269[1]

IMP: Inferred from Mutant Phenotype

P

Fig. 5BC

complete
CACAO 2729

GO:0016442

RNA-induced silencing complex

PMID:20616046[2]

IDA: Inferred from Direct Assay

C

complete
CACAO 5013

GO:0000166

nucleotide binding

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

GO:0000288

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Reactome:REACT_20639

TAS: Traceable Author Statement

P

Seeded From UniProt

complete

GO:0000932

cytoplasmic mRNA processing body

GO_REF:0000039

IEA: Inferred from Electronic Annotation

UniProtKB-SubCell:SL-0230

C

Seeded From UniProt

complete

GO:0000932

cytoplasmic mRNA processing body

PMID:16699599[3]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0000932

cytoplasmic mRNA processing body

PMID:20616046[2]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0000932

cytoplasmic mRNA processing body

PMID:20826699[4]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0000932

cytoplasmic mRNA processing body

PMID:22022269[1]

IMP: Inferred from Mutant Phenotype

C

Seeded From UniProt

complete

GO:0000932

cytoplasmic mRNA processing body

PMID:22915799[5]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0003676

nucleic acid binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011545

F

Seeded From UniProt

complete

GO:0003723

RNA binding

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0694

F

Seeded From UniProt

complete

GO:0003724

RNA helicase activity

PMID:1579499[6]

TAS: Traceable Author Statement

F

Seeded From UniProt

complete

GO:0004004

ATP-dependent RNA helicase activity

GO_REF:0000033

IBA: Inferred from Biological aspect of Ancestor

PANTHER:PTN000618218

F

Seeded From UniProt

complete

GO:0004386

helicase activity

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0347

F

Seeded From UniProt

complete

GO:0004386

helicase activity

PMID:1394235[7]

TAS: Traceable Author Statement

F

Seeded From UniProt

complete

GO:0004386

helicase activity

PMID:1579499[6]

TAS: Traceable Author Statement

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:16364915[8]

IPI: Inferred from Physical Interaction

UniProtKB:Q96F86

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:16364915[8]

IPI: Inferred from Physical Interaction

UniProtKB:Q9NPI6

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:16699599[3]

IPI: Inferred from Physical Interaction

UniProtKB:Q9HC16

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:17392519[9]

IPI: Inferred from Physical Interaction

UniProtKB:Q99700

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:17392519[9]

IPI: Inferred from Physical Interaction

UniProtKB:Q99700

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:20543818[10]

IPI: Inferred from Physical Interaction

UniProtKB:Q86TB9

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:20584987[11]

IPI: Inferred from Physical Interaction

UniProtKB:Q86TB9

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:20616046[2]

IPI: Inferred from Physical Interaction

UniProtKB:A6NIX2

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:20616046[2]

IPI: Inferred from Physical Interaction

UniProtKB:Q96IF1

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:20616046[2]

IPI: Inferred from Physical Interaction

UniProtKB:Q9UGP4

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25036637[12]

IPI: Inferred from Physical Interaction

UniProtKB:Q9NPI6

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:O94972

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:P14373

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:P15884

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:P17028

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:P60410

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q08117

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q08379

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q13137

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q13422

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q15233-2

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q59EK9

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q6A162

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q8N1B4

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q8N7W2-2

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q8NHQ1

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q96BR9

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q96C92-2

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q96CA5

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q96F86

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q96PV4

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:25416956[13]

IPI: Inferred from Physical Interaction

UniProtKB:Q9NRA8

F

Seeded From UniProt

complete

GO:0005524

ATP binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011545

F

Seeded From UniProt

complete

GO:0005524

ATP binding

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

GO:0005737

cytoplasm

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

GO:0005737

cytoplasm

GO_REF:0000052

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0005829

cytosol

Reactome:REACT_20560

TAS: Traceable Author Statement

C

Seeded From UniProt

complete

GO:0006417

regulation of translation

GO_REF:0000033

IBA: Inferred from Biological aspect of Ancestor

PANTHER:PTN000619958

P

Seeded From UniProt

complete

GO:0010467

gene expression

Reactome:REACT_71

TAS: Traceable Author Statement

P

Seeded From UniProt

complete

GO:0010494

cytoplasmic stress granule

PMID:17392519[9]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0010501

RNA secondary structure unwinding

GO_REF:0000033

IBA: Inferred from Biological aspect of Ancestor

PANTHER:PTN000618218

P

Seeded From UniProt

complete

GO:0016020

membrane

PMID:19946888[14]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0016442

RISC complex

PMID:20616046[2]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0016787

hydrolase activity

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

GO:0019074

viral RNA genome packaging

PMID:22022269[1]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0019827

stem cell maintenance

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000128421

P

Seeded From UniProt

complete

GO:0019904

protein domain specific binding

PMID:24768540[15]

IPI: Inferred from Physical Interaction

UniProtKB:A5YKK6

F

Seeded From UniProt

complete

GO:0033962

cytoplasmic mRNA processing body assembly

PMID:20826699[4]

IDA: Inferred from Direct Assay

P

Seeded From UniProt

complete

GO:0043231

intracellular membrane-bounded organelle

GO_REF:0000052

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0043928

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

Reactome:REACT_20518

TAS: Traceable Author Statement

P

Seeded From UniProt

complete

GO:0044822

poly(A) RNA binding

PMID:22658674[16]

IDA: Inferred from Direct Assay

F

Seeded From UniProt

complete

GO:0044822

poly(A) RNA binding

PMID:22681889[17]

IDA: Inferred from Direct Assay

F

Seeded From UniProt

complete

GO:0045665

negative regulation of neuron differentiation

GO_REF:0000019

IEA: Inferred from Electronic Annotation

Ensembl:ENSMUSP00000128421

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 Yu, SF et al. (2011) The DEAD-box RNA helicase DDX6 is required for efficient encapsidation of a retroviral genome. PLoS Pathog. 7 e1002303 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 2.4 2.5 James, V et al. (2010) LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-mediated gene silencing. Proc. Natl. Acad. Sci. U.S.A. 107 12499-504 PubMed GONUTS page
  3. 3.0 3.1 Wichroski, MJ et al. (2006) Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies. PLoS Pathog. 2 e41 PubMed GONUTS page
  4. 4.0 4.1 Marnef, A et al. (2010) Distinct functions of maternal and somatic Pat1 protein paralogs. RNA 16 2094-107 PubMed GONUTS page
  5. Phalora, PK et al. (2012) HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies. J. Virol. 86 11712-24 PubMed GONUTS page
  6. 6.0 6.1 Lu, D & Yunis, JJ (1992) Cloning, expression and localization of an RNA helicase gene from a human lymphoid cell line with chromosomal breakpoint 11q23.3. Nucleic Acids Res. 20 1967-72 PubMed GONUTS page
  7. Akao, Y et al. (1992) 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. Cancer Res. 52 6083-7 PubMed GONUTS page
  8. 8.0 8.1 Fenger-Grøn, M et al. (2005) Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Mol. Cell 20 905-15 PubMed GONUTS page
  9. 9.0 9.1 9.2 Nonhoff, U et al. (2007) Ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6 and interferes with P-bodies and stress granules. Mol. Biol. Cell 18 1385-96 PubMed GONUTS page
  10. Braun, JE et al. (2010) The C-terminal alpha-alpha superhelix of Pat is required for mRNA decapping in metazoa. EMBO J. 29 2368-80 PubMed GONUTS page
  11. Ozgur, S et al. (2010) Human Pat1b connects deadenylation with mRNA decapping and controls the assembly of processing bodies. Mol. Cell. Biol. 30 4308-23 PubMed GONUTS page
  12. Taipale, M et al. (2014) A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. Cell 158 434-48 PubMed GONUTS page
  13. 13.00 13.01 13.02 13.03 13.04 13.05 13.06 13.07 13.08 13.09 13.10 13.11 13.12 13.13 13.14 13.15 13.16 13.17 13.18 13.19 13.20 Rolland, T et al. (2014) A proteome-scale map of the human interactome network. Cell 159 1212-26 PubMed GONUTS page
  14. Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
  15. Chen, Y et al. (2014) A DDX6-CNOT1 complex and W-binding pockets in CNOT9 reveal direct links between miRNA target recognition and silencing. Mol. Cell 54 737-50 PubMed GONUTS page
  16. Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
  17. Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page