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Protein

Probable ATP-dependent RNA helicase DDX6

Gene

Ddx6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi140 – 1478ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. helicase activity Source: UniProtKB-KW
  3. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. cytoplasmic mRNA processing body assembly Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_330258. mRNA decay by 5' to 3' exoribonuclease.

Names & Taxonomyi

Protein namesi
Recommended 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 homolog
Gene namesi
Name:Ddx6
Synonyms:Hlr2, Rck
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:104976. Ddx6.

Subcellular locationi

CytoplasmP-body By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytoplasmic mRNA processing body Source: MGI
  3. cytoplasmic stress granule Source: Ensembl
  4. intracellular membrane-bounded organelle Source: Ensembl
  5. membrane Source: Ensembl
  6. RISC complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483Probable ATP-dependent RNA helicase DDX6PRO_0000054984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP54823.
PaxDbiP54823.
PRIDEiP54823.

PTM databases

PhosphoSiteiP54823.

Expressioni

Developmental stagei

Abundant expression in growing oocytes, levels decline in primary and secondary oocytes, and degradation appears to be complete by the mid-late two-cell stage.1 Publication

Gene expression databases

BgeeiP54823.
CleanExiMM_DDX6.
GenevestigatoriP54823.

Interactioni

Subunit structurei

Forms a complex with DCP1A, DCP2, EDC3 and EDC4/HEDLS (By similarity). Interacts with LIMD1, WTIP and AJUBA (By similarity). Interacts with APOBEC3G in an RNA-dependent manner (By similarity). Interacts with RC3H1.By similarity1 Publication

Protein-protein interaction databases

BioGridi199087. 2 interactions.
IntActiP54823. 5 interactions.
MINTiMINT-4093002.

Structurei

3D structure databases

ProteinModelPortaliP54823.
SMRiP54823. Positions 95-469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini127 – 298172Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini308 – 468161Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi96 – 12429Q motifAdd
BLAST
Motifi246 – 2494DEAD box

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00740000115573.
HOGENOMiHOG000268797.
HOVERGENiHBG106685.
InParanoidiP54823.
KOiK12614.
OMAiRIYQKVQ.
OrthoDBiEOG7D85W7.
PhylomeDBiP54823.
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.

P54823-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTARTENPV IMGLSSQNGQ LRGPVKASAG PGGGGTQPQP QLNQLKNTST
60 70 80 90 100
INNGTPQQAQ SMAATIKPGD 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 AEYHSEPAED EKP
Length:483
Mass (Da):54,192
Last modified:October 1, 1996 - v1
Checksum:i9AD22D171F8BC14D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 425PQPQL → TQQQM in AAB94769 (PubMed:9883581).Curated
Sequence conflicti202 – 2021G → P in AAB94769 (PubMed:9883581).Curated
Sequence conflicti241 – 2411Q → R in BAC35670 (PubMed:15489334).Curated
Sequence conflicti311 – 3111Q → E in BAC35670 (PubMed:15489334).Curated
Sequence conflicti381 – 3811R → E in AAB94769 (PubMed:9883581).Curated
Sequence conflicti407 – 4071I → M in BAC35670 (PubMed:15489334).Curated
Sequence conflicti422 – 4221I → V in AAB94769 (PubMed:9883581).Curated
Sequence conflicti478 – 4781A → V in AAB94769 (PubMed:9883581).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50494 mRNA. Translation: BAA09088.1.
AK054144 mRNA. Translation: BAC35670.1.
AK148483 mRNA. Translation: BAE28578.1.
BC021452 mRNA. Translation: AAH21452.1.
AF038995 mRNA. Translation: AAB94769.1.
CCDSiCCDS23116.1.
RefSeqiNP_001104296.1. NM_001110826.1.
NP_031867.1. NM_007841.4.
NP_851841.2. NM_181324.3.
UniGeneiMm.267061.

Genome annotation databases

EnsembliENSMUST00000170489; ENSMUSP00000128421; ENSMUSG00000032097.
GeneIDi13209.
KEGGimmu:13209.
UCSCiuc009pdy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50494 mRNA. Translation: BAA09088.1.
AK054144 mRNA. Translation: BAC35670.1.
AK148483 mRNA. Translation: BAE28578.1.
BC021452 mRNA. Translation: AAH21452.1.
AF038995 mRNA. Translation: AAB94769.1.
CCDSiCCDS23116.1.
RefSeqiNP_001104296.1. NM_001110826.1.
NP_031867.1. NM_007841.4.
NP_851841.2. NM_181324.3.
UniGeneiMm.267061.

3D structure databases

ProteinModelPortaliP54823.
SMRiP54823. Positions 95-469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199087. 2 interactions.
IntActiP54823. 5 interactions.
MINTiMINT-4093002.

PTM databases

PhosphoSiteiP54823.

Proteomic databases

MaxQBiP54823.
PaxDbiP54823.
PRIDEiP54823.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000170489; ENSMUSP00000128421; ENSMUSG00000032097.
GeneIDi13209.
KEGGimmu:13209.
UCSCiuc009pdy.2. mouse.

Organism-specific databases

CTDi1656.
MGIiMGI:104976. Ddx6.

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00740000115573.
HOGENOMiHOG000268797.
HOVERGENiHBG106685.
InParanoidiP54823.
KOiK12614.
OMAiRIYQKVQ.
OrthoDBiEOG7D85W7.
PhylomeDBiP54823.
TreeFamiTF300440.

Enzyme and pathway databases

ReactomeiREACT_330258. mRNA decay by 5' to 3' exoribonuclease.

Miscellaneous databases

NextBioi283376.
PROiP54823.
SOURCEiSearch...

Gene expression databases

BgeeiP54823.
CleanExiMM_DDX6.
GenevestigatoriP54823.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a murine cDNA homologous to the human RCK/P54, a lymphoma-linked chromosomal translocation junction gene on 11q23."
    Seto M., Yamamoto K., Takahashi T., Ueda R.
    Gene 166:293-296(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Spleen.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Oviduct and Pancreas.
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  4. "RNA-binding proteins in mouse oocytes and embryos: expression of genes encoding Y box, DEAD box RNA helicase, and polyA binding proteins."
    Paynton B.V.
    Dev. Genet. 23:285-298(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-478, DEVELOPMENTAL STAGE.
    Strain: CB6F1/J.
    Tissue: Oocyte.
  5. "Roquin binds inducible costimulator mRNA and effectors of mRNA decay to induce microRNA-independent post-transcriptional repression."
    Glasmacher E., Hoefig K.P., Vogel K.U., Rath N., Du L., Wolf C., Kremmer E., Wang X., Heissmeyer V.
    Nat. Immunol. 11:725-733(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RC3H1.

Entry informationi

Entry nameiDDX6_MOUSE
AccessioniPrimary (citable) accession number: P54823
Secondary accession number(s): O54979, Q3UFI3, Q8BW68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 1, 2015
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.