Probable ATP-dependent RNA helicase DDX6

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Reviewed, UniProtKB/Swiss-Prot P26196 (DDX6_HUMAN)

Last modified June 16, 2009. Version 100. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Probable ATP-dependent RNA helicase DDX6
    EC=3.6.1.-
Alternative name(s):
    DEAD box protein 6
    ATP-dependent RNA helicase p54
    Oncogene RCK

Gene names

Name:	DDX6
Synonyms:	HLR2, RCK

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	483 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	In the process of mRNA degradation, may play a role in mRNA decapping.
Subunit structure	Forms a complex with DCP1A, DCP2, EDC3 and EDC4/HEDLS.
Subcellular location	Cytoplasm › P-body. Note: Processing bodies (PB). Ref.4
Tissue specificity	Abundantly expressed in most tissues.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.5
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.

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Chromosomal rearrangement
Disease	Proto-oncogene
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Cellular component	cytoplasmic mRNA processing body Inferred from electronic annotation. Source: UniProtKB-SubCell stress granule Inferred from direct assay. Source: UniProtKB
Molecular function	ATP 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 Ref.1 Traceable author statement. Source: ProtInc protein binding Ref.4 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
DCP1A	Q9NPI6	1	EBI-351257,EBI-374238
EDC3	Q96F86	1	EBI-351257,EBI-997311
POLR1E	Q9GZS1	1	EBI-351257,EBI-359458
YWHAQ	P27348	1	EBI-351257,EBI-359854

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 483

483

Probable ATP-dependent RNA helicase DDX6

PRO_0000054983

Regions

Domain

127 – 298

172

Helicase ATP-binding

Domain

308 – 468

161

Helicase C-terminal

Nucleotide binding

140 – 147

ATP By similarity

Motif

96 – 124

Q motif

Motif

246 – 249

DEAD box

Amino acid modifications

Modified residue

Phosphothreonine Ref.5

Experimental info

Sequence conflict

293

Q → E in Z11685. Ref.1

Secondary structure

483

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P26196-1 [UniParc].

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

483

54,417

        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

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References

	« Hide 'large scale' referencesShow '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: 1579499] [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: 15489334] [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: 1394235] [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: 16364915] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DCP1A; DCP2; EDC3 AND EDC4, SUBCELLULAR LOCATION.
[5]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, MASS SPECTROMETRY.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"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: 14684915] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 94-299.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

Z11685 mRNA. No translation available.
BC065007 mRNA. Translation: AAH65007.1.
D17532 mRNA. Translation: BAA04482.1.

IPI

IPI00030320.

PIR

S22651.

RefSeq

NP_004388.2.

UniGene

Hs.654366

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VEC	X-ray	2.01	A/B	94-299	[»]
2WAX	X-ray	2.30	A/C	296-483	[»]
2WAY	X-ray	2.30	A/C	296-483	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:29195N.

IntAct

P26196. 10 interactions.

PTM databases

PhosphoSite

P26196.

2-D gel databases

DOSAC-COBS-2DPAGE

P26196.

Proteomic databases

PeptideAtlas

P26196.

PRIDE

P26196.

Genome annotation databases

Ensembl

ENSG00000110367. Homo sapiens. [Contig view]

GeneID

1656.

KEGG

hsa:1656.

Organism-specific databases

GeneCards

GC11M118125.

HGNC

HGNC:2747. DDX6.

HPA

CAB004668.

MIM

600326. gene.

PharmGKB

PA27229.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P26196.

HOVERGEN

P26196.

OMA

P26196. YKIEQEL.

Gene expression databases

ArrayExpress

P26196.

Bgee

P26196.

CleanEx

HS_DDX6.

GermOnline

ENSG00000110367. Homo sapiens.

Family and domain databases

InterPro

IPR014001. DEAD-like_N.
IPR001650. DNA/RNA_helicase_C.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]

Pfam

PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

PROSITE

PS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

6820.

SOURCE

Search...

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Entry information

Entry name

DDX6_HUMAN

Accession

Primary (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:	June 16, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 11

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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents