Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable ATP-dependent RNA helicase DDX6

Gene

DDX6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In the process of mRNA degradation, plays a role in mRNA decapping (PubMed:16364915). Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degration of their transcripts (PubMed:26098573).2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.Curated

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi140 – 147ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: GO_Central
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • helicase activity Source: ProtInc
  • poly(A) RNA binding Source: UniProtKB
  • protein domain specific binding Source: BHF-UCL
  • RNA helicase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000110367-MONOMER.
BRENDAi3.6.4.13. 2681.
ReactomeiR-HSA-430039. mRNA decay by 5' to 3' exoribonuclease.
SIGNORiP26196.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ATP-dependent RNA helicase DDX6Curated (EC:3.6.4.13Curated)
Alternative name(s):
ATP-dependent RNA helicase p54
DEAD box protein 6
Oncogene RCK
Gene namesi
Name:DDX6
Synonyms:HLR2, RCK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:2747. DDX6.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytoplasmic stress granule Source: UniProtKB
  • cytosol Source: Reactome
  • heterochromatin Source: Ensembl
  • intracellular membrane-bounded organelle Source: HPA
  • membrane Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nucleolus Source: Ensembl
  • nucleus Source: UniProtKB
  • outer dense fiber Source: Ensembl
  • P granule Source: Ensembl
  • RISC complex Source: MGI
  • sperm annulus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi320Q → A: Abolishes interaction with EDC3; when associated with A-323; A-327 and A-331. 1 Publication1
Mutagenesisi323H → A: Abolishes interaction with EDC3; when associated with A-320; A-327 and A-331. 1 Publication1
Mutagenesisi327T → A: Abolishes interaction with EDC3; when associated with A-320; A-323 and A-331. 1 Publication1
Mutagenesisi331R → A: Abolishes interaction with EDC3; when associated with A-320; A-323 and A-327. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi1656.
OpenTargetsiENSG00000110367.
PharmGKBiPA27229.

Polymorphism and mutation databases

BioMutaiDDX6.
DMDMi116241327.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000549831 – 483Probable ATP-dependent RNA helicase DDX6Add BLAST483

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei36PhosphothreonineCombined sources1

Post-translational modificationi

Sumoylated (PubMed:26184334).1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP26196.
MaxQBiP26196.
PaxDbiP26196.
PeptideAtlasiP26196.
PRIDEiP26196.

2D gel databases

DOSAC-COBS-2DPAGEP26196.

PTM databases

iPTMnetiP26196.
PhosphoSitePlusiP26196.
SwissPalmiP26196.

Expressioni

Tissue specificityi

Abundantly expressed in most tissues.

Gene expression databases

BgeeiENSG00000110367.
CleanExiHS_DDX6.
ExpressionAtlasiP26196. baseline and differential.
GenevisibleiP26196. HS.

Organism-specific databases

HPAiCAB004668.
HPA024201.
HPA026644.

Interactioni

Subunit structurei

Forms a complex with DCP1A, DCP2, EDC3 and EDC4/HEDLS (PubMed:16364915, PubMed:19285948). Interacts with LIMD1, WTIP and AJUBA (PubMed:20616046). Interacts with APOBEC3G in an RNA-dependent manner (PubMed:16699599). Interacts with RC3H1 (By similarity). Interacts with ATXN2L (PubMed:23209657). Interacts with MCRIP1 (PubMed:26184334). Interacts with MCRIP2 (PubMed:26184334). Interacts with NUFIP2 (PubMed:26184334).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AESQ081173EBI-351257,EBI-717810
ATXN2Q997007EBI-351257,EBI-697691
BEND7Q8N7W2-23EBI-351257,EBI-10181188
BIRC7Q96CA55EBI-351257,EBI-517623
CALCOCO2Q131375EBI-351257,EBI-739580
CEP70Q8NHQ15EBI-351257,EBI-739624
DCP1AQ9NPI66EBI-351257,EBI-374238
EDC3Q96F869EBI-351257,EBI-997311
EIF4ENIF1Q9NRA85EBI-351257,EBI-301024
GOLGA2Q083793EBI-351257,EBI-618309
IKZF1Q134223EBI-351257,EBI-745305
KRT40Q6A1623EBI-351257,EBI-10171697
KRTAP10-8P604105EBI-351257,EBI-10171774
NONOQ15233-23EBI-351257,EBI-10203843
PNMA5Q96PV43EBI-351257,EBI-10171633
RUNDC3AQ59EK93EBI-351257,EBI-747225
SDCCAG3Q96C92-23EBI-351257,EBI-10178036
SIPA1L2Q9P2F8-24EBI-351257,EBI-10326741
TCF4P158843EBI-351257,EBI-533224
TRIM27P143735EBI-351257,EBI-719493
TRIM37O949723EBI-351257,EBI-741602
VPS52Q8N1B45EBI-351257,EBI-2799833
ZBTB8AQ96BR95EBI-351257,EBI-742740
ZNF24P170283EBI-351257,EBI-707773

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • protein domain specific binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108022. 85 interactors.
DIPiDIP-29195N.
IntActiP26196. 93 interactors.
MINTiMINT-5004149.
STRINGi9606.ENSP00000264018.

Structurei

Secondary structure

1483
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi98 – 100Combined sources3
Helixi105 – 112Combined sources8
Turni113 – 115Combined sources3
Helixi121 – 131Combined sources11
Beta strandi136 – 139Combined sources4
Beta strandi142 – 144Combined sources3
Helixi147 – 157Combined sources11
Beta strandi167 – 170Combined sources4
Helixi174 – 187Combined sources14
Turni188 – 190Combined sources3
Beta strandi191 – 193Combined sources3
Beta strandi196 – 199Combined sources4
Beta strandi201 – 203Combined sources3
Helixi205 – 211Combined sources7
Beta strandi217 – 221Combined sources5
Helixi223 – 231Combined sources9
Beta strandi242 – 247Combined sources6
Helixi248 – 251Combined sources4
Turni254 – 256Combined sources3
Helixi257 – 266Combined sources10
Beta strandi272 – 278Combined sources7
Helixi282 – 291Combined sources10
Beta strandi296 – 298Combined sources3
Beta strandi309 – 315Combined sources7
Helixi318 – 320Combined sources3
Helixi321 – 331Combined sources11
Beta strandi335 – 340Combined sources6
Helixi344 – 356Combined sources13
Beta strandi361 – 364Combined sources4
Beta strandi366 – 368Combined sources3
Helixi370 – 381Combined sources12
Beta strandi384 – 390Combined sources7
Helixi397 – 399Combined sources3
Beta strandi403 – 410Combined sources8
Helixi415 – 422Combined sources8
Helixi423 – 425Combined sources3
Beta strandi432 – 438Combined sources7
Helixi440 – 442Combined sources3
Helixi443 – 453Combined sources11
Helixi462 – 465Combined sources4
Helixi466 – 468Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VECX-ray2.01A/B94-299[»]
2WAXX-ray2.30A/C296-483[»]
2WAYX-ray2.30A/C296-483[»]
4CRWX-ray1.75B307-483[»]
4CT4X-ray2.30B/D95-469[»]
4CT5X-ray3.00A/B95-469[»]
5ANRX-ray2.10B95-469[»]
ProteinModelPortaliP26196.
SMRiP26196.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26196.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini127 – 298Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST172
Domaini308 – 468Helicase C-terminalPROSITE-ProRule annotationAdd BLAST161

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi96 – 124Q motifAdd BLAST29
Motifi246 – 249DEAD box4

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0326. Eukaryota.
ENOG410XRAZ. LUCA.
GeneTreeiENSGT00860000133781.
HOGENOMiHOG000268797.
HOVERGENiHBG106685.
InParanoidiP26196.
KOiK12614.
OMAiIYQKVQV.
OrthoDBiEOG091G0623.
PhylomeDBiP26196.
TreeFamiTF300440.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26196-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTARTENPV IMGLSSQNGQ LRGPVKPTGG PGGGGTQTQQ QMNQLKNTNT
60 70 80 90 100
INNGTQQQAQ SMTTTIKPGD DWKKTLKLPP KDLRIKTSDV TSTKGNEFED
110 120 130 140 150
YCLKRELLMG IFEMGWEKPS PIQEESIPIA LSGRDILARA KNGTGKSGAY
160 170 180 190 200
LIPLLERLDL KKDNIQAMVI VPTRELALQV SQICIQVSKH MGGAKVMATT
210 220 230 240 250
GGTNLRDDIM RLDDTVHVVI ATPGRILDLI KKGVAKVDHV QMIVLDEADK
260 270 280 290 300
LLSQDFVQIM EDIILTLPKN RQILLYSATF PLSVQKFMNS HLQKPYEINL
310 320 330 340 350
MEELTLKGVT QYYAYVTERQ KVHCLNTLFS RLQINQSIIF CNSSQRVELL
360 370 380 390 400
AKKISQLGYS CFYIHAKMRQ EHRNRVFHDF RNGLCRNLVC TDLFTRGIDI
410 420 430 440 450
QAVNVVINFD FPKLAETYLH RIGRSGRFGH LGLAINLITY DDRFNLKSIE
460 470 480
EQLGTEIKPI PSNIDKSLYV AEYHSEPVED EKP
Length:483
Mass (Da):54,417
Last modified:October 17, 2006 - v2
Checksum:iF802C642861793FB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti293Q → E in Z11685 (PubMed:1579499).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11685 mRNA. No translation available.
BC065007 mRNA. Translation: AAH65007.1.
D17532 mRNA. Translation: BAA04482.1.
CCDSiCCDS44751.1.
PIRiS22651.
RefSeqiNP_001244120.1. NM_001257191.2.
NP_004388.2. NM_004397.5.
XP_005271474.1. XM_005271417.3.
UniGeneiHs.408461.

Genome annotation databases

EnsembliENST00000526070; ENSP00000433704; ENSG00000110367.
ENST00000534980; ENSP00000442266; ENSG00000110367.
ENST00000620157; ENSP00000478754; ENSG00000110367.
GeneIDi1656.
KEGGihsa:1656.
UCSCiuc031ygs.2. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11685 mRNA. No translation available.
BC065007 mRNA. Translation: AAH65007.1.
D17532 mRNA. Translation: BAA04482.1.
CCDSiCCDS44751.1.
PIRiS22651.
RefSeqiNP_001244120.1. NM_001257191.2.
NP_004388.2. NM_004397.5.
XP_005271474.1. XM_005271417.3.
UniGeneiHs.408461.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VECX-ray2.01A/B94-299[»]
2WAXX-ray2.30A/C296-483[»]
2WAYX-ray2.30A/C296-483[»]
4CRWX-ray1.75B307-483[»]
4CT4X-ray2.30B/D95-469[»]
4CT5X-ray3.00A/B95-469[»]
5ANRX-ray2.10B95-469[»]
ProteinModelPortaliP26196.
SMRiP26196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108022. 85 interactors.
DIPiDIP-29195N.
IntActiP26196. 93 interactors.
MINTiMINT-5004149.
STRINGi9606.ENSP00000264018.

PTM databases

iPTMnetiP26196.
PhosphoSitePlusiP26196.
SwissPalmiP26196.

Polymorphism and mutation databases

BioMutaiDDX6.
DMDMi116241327.

2D gel databases

DOSAC-COBS-2DPAGEP26196.

Proteomic databases

EPDiP26196.
MaxQBiP26196.
PaxDbiP26196.
PeptideAtlasiP26196.
PRIDEiP26196.

Protocols and materials databases

DNASUi1656.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000526070; ENSP00000433704; ENSG00000110367.
ENST00000534980; ENSP00000442266; ENSG00000110367.
ENST00000620157; ENSP00000478754; ENSG00000110367.
GeneIDi1656.
KEGGihsa:1656.
UCSCiuc031ygs.2. human.

Organism-specific databases

CTDi1656.
DisGeNETi1656.
GeneCardsiDDX6.
HGNCiHGNC:2747. DDX6.
HPAiCAB004668.
HPA024201.
HPA026644.
MIMi600326. gene.
neXtProtiNX_P26196.
OpenTargetsiENSG00000110367.
PharmGKBiPA27229.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0326. Eukaryota.
ENOG410XRAZ. LUCA.
GeneTreeiENSGT00860000133781.
HOGENOMiHOG000268797.
HOVERGENiHBG106685.
InParanoidiP26196.
KOiK12614.
OMAiIYQKVQV.
OrthoDBiEOG091G0623.
PhylomeDBiP26196.
TreeFamiTF300440.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000110367-MONOMER.
BRENDAi3.6.4.13. 2681.
ReactomeiR-HSA-430039. mRNA decay by 5' to 3' exoribonuclease.
SIGNORiP26196.

Miscellaneous databases

ChiTaRSiDDX6. human.
EvolutionaryTraceiP26196.
GeneWikiiDDX6.
GenomeRNAii1656.
PROiP26196.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000110367.
CleanExiHS_DDX6.
ExpressionAtlasiP26196. baseline and differential.
GenevisibleiP26196. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDDX6_HUMAN
AccessioniPrimary (citable) accession number: P26196
Secondary accession number(s): Q5D048
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 181 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.