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Protein

ATP-dependent DNA helicase DDX11

Gene

Ddx11

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

Functioni

DNA-dependent ATPase and ATP-dependent DNA helicase that participates in various functions in genomic stability, including DNA replication, DNA repair and heterochromatin organization as well as in ribosomal RNA synthesis. Its double-stranded DNA helicase activity requires either a minimal 5'-single-stranded tail length of approximately 15 nt (flap substrates) or 10 nt length single-stranded gapped DNA substrates of a partial duplex DNA structure for helicase loading and translocation along DNA in a 5' to 3' direction. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended up to 500 bp by the replication protein A (RPA) or the cohesion CTF18-replication factor C (Ctf18-RFC) complex activities. Shows also ATPase- and helicase activities on substrates that mimic key DNA intermediates of replication, repair and homologous recombination reactions, including forked duplex, anti-parallel G-quadruplex and three-stranded D-loop DNA molecules. Plays a role in DNA double-strand break (DSB) repair at the DNA replication fork during DNA replication recovery from DNA damage. Recruited with TIMELESS factor upon DNA-replication stress response at DNA replication fork to preserve replication fork progression, and hence ensure DNA replication fidelity (By similarity). Cooperates also with TIMELESS factor during DNA replication to regulate proper sister chromatid cohesion and mitotic chromosome segregation (PubMed:17611414). Stimulates 5'-single-stranded DNA flap endonuclease activity of FEN1 in an ATP- and helicase-independent manner; and hence it may contribute in Okazaki fragment processing at DNA replication fork during lagging strand DNA synthesis. Its ability to function at DNA replication fork is modulated by its binding to long non-coding RNA (lncRNA) cohesion regulator non-coding RNA DDX11-AS1/CONCR, which is able to increase both DDX11 ATPase activity and binding to DNA replicating regions (By similarity). Plays also a role in heterochromatin organization (PubMed:21854770). Involved in rRNA transcription activation through binding to active hypomethylated rDNA gene loci by recruiting UBTF and the RNA polymerase Pol I transcriptional machinery (By similarity). Plays a role in embryonic development and prevention of aneuploidy (PubMed:17611414). Involved in melanoma cell proliferation and survival. Associates with chromatin at DNA replication fork regions. Binds to single- and double-stranded DNAs (By similarity).By similarity2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.By similarity

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi239Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi257Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi286Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi321Iron-sulfur (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi44 – 51ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, Transcription, Transcription regulation

Keywords - Ligandi

4Fe-4S, ATP-binding, DNA-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent DNA helicase DDX11Curated (EC:3.6.4.12By similarity)
Alternative name(s):
DEAD/H-box protein 11Imported
Gene namesi
Name:Ddx11Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:2443590. Ddx11.

Subcellular locationi

  • Nucleus By similarity
  • Nucleusnucleolus By similarity
  • Cytoplasmcytoskeletonspindle pole By similarity
  • Midbody By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity

  • Note: During the early stages of mitosis, localizes to condensed chromatin and is released from the chromatin with progression to metaphase. Also localizes to the spindle poles throughout mitosis and at the midbody at later stages of mitosis (metaphase to telophase). In interphase, colocalizes with nucleolin in the nucleolus.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryonic death at 10.5 dpc (PubMed:17611414). Embryos are smaller in size, malformed and exhibit sparse cellularity in comparison to normal or heterozygous litter mates (PubMed:17611414). Show inability to form a proper embryonic placenta. Display high incidence of cell aneuploidy due to abnormal chromosomal segregation (PubMed:17611414). Show abnormal formation and localization of heterochromatin (PubMed:21854770).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000551371 – 880ATP-dependent DNA helicase DDX11Add BLAST880

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei234PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6AXC6.
MaxQBiQ6AXC6.
PaxDbiQ6AXC6.
PeptideAtlasiQ6AXC6.
PRIDEiQ6AXC6.

PTM databases

iPTMnetiQ6AXC6.
PhosphoSitePlusiQ6AXC6.

Expressioni

Gene expression databases

BgeeiENSMUSG00000035842.
GenevisibleiQ6AXC6. MM.

Interactioni

Subunit structurei

Associates with the CTF18-RFC complex. Associates with a cohesin complex composed of RAD21, SMC1 proteins and SMC3. Interacts with CHTF18. Interacts with DSCC1. Interacts with FEN1; this interaction is direct and increases flap endonuclease activity of FEN1. Interacts with PCNA. Interacts with POLR1A and UBTF. Interacts with RAD21, SMC1 proteins and SMC3. Interacts with RFC2. Interacts with TIMELESS; this interaction increases recruitment of both proteins onto chromatin in response to replication stress induction by hydroxyurea.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000130440.

Structurei

3D structure databases

ProteinModelPortaliQ6AXC6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 416Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST408

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi364 – 367DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi121 – 196Glu-richAdd BLAST76

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1133. Eukaryota.
COG1199. LUCA.
GeneTreeiENSGT00530000063199.
HOGENOMiHOG000241266.
HOVERGENiHBG058884.
InParanoidiQ6AXC6.
KOiK11273.
OMAiNLCQVIP.
OrthoDBiEOG091G034C.
PhylomeDBiQ6AXC6.
TreeFamiTF300435.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR006555. ATP-dep_Helicase_C.
IPR010614. DEAD_2.
IPR013020. DNA_helicase_DNA-repair_Rad3.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF06733. DEAD_2. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
SMARTiSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00604. rad3. 1 hit.
PROSITEiPS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6AXC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADENQEIGG IHFPFPFPPY PIQKDFMAEL YKVLEGGKIG IFESPTGTGK
60 70 80 90 100
SLSLICGALS WLRDFEKKKL QAEALLLAPG SGPPSSEKNS LLTSSSCQEP
110 120 130 140 150
TDTPRPAGEP DWVTEFVQKK EERDLVERLR EEQKHEEEET EALLRLSREM
160 170 180 190 200
LDAGTGPEQL EQLECGEEHL VLAEYESDEE RRGSRVDEAE DDLEEEHITK
210 220 230 240 250
IYYCSRTHSQ LAQFVREVLK SPFGKETRLV SLGSRQTLCV NEDVKNLGSV
260 270 280 290 300
QLMNDRCVDM QRSKREKNGT GEDKPKRKRQ KIQTSCPFYN HEQMELLRDE
310 320 330 340 350
ILLEVKDMEQ LVALGKEARA CPYYGSRFAI PAAQLVVLPY PMLLHAATRQ
360 370 380 390 400
AAGIRLQGQV VIIDEAHNLI DTITNIHSTE VNGSQLCQAH SQLLQYMERY
410 420 430 440 450
RKRLKAKNLM YIKQILYLLE KFVAVLGGNV KQNPTTQSLS QTGSELKSIN
460 470 480 490 500
DFLFQSQVDN INLFKVQRYL EKSMLSRKLF GFTECFGVVL PSLSDSQENR
510 520 530 540 550
GLAGFQQFLK SLQSGPTEDS PEEGQAVALR PASPLMHIEA FLAALTTANQ
560 570 580 590 600
DGRVIVNRQG SVGQSSLKFL LLNPAVHFAQ VVKECRAVVI AGGTMQPMSD
610 620 630 640 650
FREQLLACSG VEAGRVVEFS CGHVIPPDNI LPLIICSGPS NQQLEFTYQR
660 670 680 690 700
RELPQMVEET GRILCNLCNV VPGGVVCFLP SYEYLRQVHA HWDKTGLLTR
710 720 730 740 750
LSVRKKIFQE PKRASQVEQV LMAYSKCIMS CSHSEGHLTG ALLLSVVGGK
760 770 780 790 800
MSEGINFSDD LGRCVVMVGM PYPNIKSPEL QEKMAYLNQT LPRTQGQPLP
810 820 830 840 850
GTVLIENLCM KAINQSIGRA IRHQRDFASI VLLDHRYARP SILAKLPAWI
860 870 880
RDRVEVKATF GPAFAAVRKF HREKSHPSLV
Length:880
Mass (Da):98,728
Last modified:September 13, 2004 - v1
Checksum:i0A283D952B974F82
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079656 mRNA. Translation: AAH79656.1.
CCDSiCCDS28945.1.
RefSeqiNP_001003919.1. NM_001003919.1.
UniGeneiMm.259605.

Genome annotation databases

EnsembliENSMUST00000163605; ENSMUSP00000130440; ENSMUSG00000035842.
GeneIDi320209.
KEGGimmu:320209.
UCSCiuc008dha.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079656 mRNA. Translation: AAH79656.1.
CCDSiCCDS28945.1.
RefSeqiNP_001003919.1. NM_001003919.1.
UniGeneiMm.259605.

3D structure databases

ProteinModelPortaliQ6AXC6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000130440.

PTM databases

iPTMnetiQ6AXC6.
PhosphoSitePlusiQ6AXC6.

Proteomic databases

EPDiQ6AXC6.
MaxQBiQ6AXC6.
PaxDbiQ6AXC6.
PeptideAtlasiQ6AXC6.
PRIDEiQ6AXC6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000163605; ENSMUSP00000130440; ENSMUSG00000035842.
GeneIDi320209.
KEGGimmu:320209.
UCSCiuc008dha.1. mouse.

Organism-specific databases

CTDi1663.
MGIiMGI:2443590. Ddx11.

Phylogenomic databases

eggNOGiKOG1133. Eukaryota.
COG1199. LUCA.
GeneTreeiENSGT00530000063199.
HOGENOMiHOG000241266.
HOVERGENiHBG058884.
InParanoidiQ6AXC6.
KOiK11273.
OMAiNLCQVIP.
OrthoDBiEOG091G034C.
PhylomeDBiQ6AXC6.
TreeFamiTF300435.

Miscellaneous databases

PROiQ6AXC6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000035842.
GenevisibleiQ6AXC6. MM.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR006555. ATP-dep_Helicase_C.
IPR010614. DEAD_2.
IPR013020. DNA_helicase_DNA-repair_Rad3.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF06733. DEAD_2. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
SMARTiSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00604. rad3. 1 hit.
PROSITEiPS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDDX11_MOUSE
AccessioniPrimary (citable) accession number: Q6AXC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 13, 2004
Last modified: November 30, 2016
This is version 109 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

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.