DDX11_MOUSE
ID DDX11_MOUSE Reviewed; 906 AA.
AC Q6AXC6; A0A286YDJ5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ATP-dependent DNA helicase DDX11 {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q96FC9};
DE AltName: Full=DEAD/H-box protein 11 {ECO:0000312|MGI:MGI:2443590};
GN Name=Ddx11 {ECO:0000312|MGI:MGI:2443590};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17611414; DOI=10.4161/cc.6.13.4411;
RA Inoue A., Li T., Roby S.K., Valentine M.B., Inoue M., Boyd K., Kidd V.J.,
RA Lahti J.M.;
RT "Loss of ChlR1 helicase in mouse causes lethality due to the accumulation
RT of aneuploid cells generated by cohesion defects and placental
RT malformation.";
RL Cell Cycle 6:1646-1654(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21854770; DOI=10.1016/j.yexcr.2011.08.006;
RA Inoue A., Hyle J., Lechner M.S., Lahti J.M.;
RT "Mammalian ChlR1 has a role in heterochromatin organization.";
RL Exp. Cell Res. 317:2522-2535(2011).
CC -!- FUNCTION: DNA-dependent ATPase and ATP-dependent DNA helicase that
CC participates in various functions in genomic stability, including DNA
CC replication, DNA repair and heterochromatin organization as well as in
CC ribosomal RNA synthesis. Its double-stranded DNA helicase activity
CC requires either a minimal 5'-single-stranded tail length of
CC approximately 15 nt (flap substrates) or 10 nt length single-stranded
CC gapped DNA substrates of a partial duplex DNA structure for helicase
CC loading and translocation along DNA in a 5' to 3' direction. The
CC helicase activity is capable of displacing duplex regions up to 100 bp,
CC which can be extended up to 500 bp by the replication protein A (RPA)
CC or the cohesion CTF18-replication factor C (Ctf18-RFC) complex
CC activities. Shows also ATPase- and helicase activities on substrates
CC that mimic key DNA intermediates of replication, repair and homologous
CC recombination reactions, including forked duplex, anti-parallel G-
CC quadruplex and three-stranded D-loop DNA molecules. Plays a role in DNA
CC double-strand break (DSB) repair at the DNA replication fork during DNA
CC replication recovery from DNA damage. Recruited with TIMELESS factor
CC upon DNA-replication stress response at DNA replication fork to
CC preserve replication fork progression, and hence ensure DNA replication
CC fidelity (By similarity). Cooperates also with TIMELESS factor during
CC DNA replication to regulate proper sister chromatid cohesion and
CC mitotic chromosome segregation (PubMed:17611414). Stimulates 5'-single-
CC stranded DNA flap endonuclease activity of FEN1 in an ATP- and
CC helicase-independent manner; and hence it may contribute in Okazaki
CC fragment processing at DNA replication fork during lagging strand DNA
CC synthesis. Its ability to function at DNA replication fork is modulated
CC by its binding to long non-coding RNA (lncRNA) cohesion regulator non-
CC coding RNA DDX11-AS1/CONCR, which is able to increase both DDX11 ATPase
CC activity and binding to DNA replicating regions (By similarity). Plays
CC also a role in heterochromatin organization (PubMed:21854770). Involved
CC in rRNA transcription activation through binding to active
CC hypomethylated rDNA gene loci by recruiting UBTF and the RNA polymerase
CC Pol I transcriptional machinery (By similarity). Plays a role in
CC embryonic development and prevention of aneuploidy (PubMed:17611414).
CC Involved in melanoma cell proliferation and survival. Associates with
CC chromatin at DNA replication fork regions. Binds to single- and double-
CC stranded DNAs (By similarity). {ECO:0000250|UniProtKB:Q96FC9,
CC ECO:0000269|PubMed:17611414, ECO:0000269|PubMed:21854770}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q96FC9};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- SUBUNIT: Associates with the CTF18-RFC complex. Associates with a
CC cohesin complex composed of RAD21, SMC1 proteins and SMC3. Interacts
CC with CHTF18. Interacts with DSCC1. Interacts with FEN1; this
CC interaction is direct and increases flap endonuclease activity of FEN1.
CC Interacts with PCNA. Interacts with POLR1A and UBTF. Interacts with
CC RAD21, SMC1 proteins and SMC3. Interacts with RFC2. Interacts with
CC TIMELESS; this interaction increases recruitment of both proteins onto
CC chromatin in response to replication stress induction by hydroxyurea.
CC {ECO:0000250|UniProtKB:Q96FC9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96FC9}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q96FC9}. Cytoplasm, cytoskeleton,
CC spindle pole {ECO:0000250|UniProtKB:Q96FC9}. Midbody
CC {ECO:0000250|UniProtKB:Q96FC9}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q96FC9}.
CC Note=During the early stages of mitosis, localizes to condensed
CC chromatin and is released from the chromatin with progression to
CC metaphase. Also localizes to the spindle poles throughout mitosis and
CC at the midbody at later stages of mitosis (metaphase to telophase). In
CC interphase, colocalizes with nucleolin in the nucleolus.
CC {ECO:0000250|UniProtKB:Q96FC9}.
CC -!- DISRUPTION PHENOTYPE: Embryonic death at 10.5 dpc (PubMed:17611414).
CC Embryos are smaller in size, malformed and exhibit sparse cellularity
CC in comparison to normal or heterozygous litter mates (PubMed:17611414).
CC Show inability to form a proper embryonic placenta. Display high
CC incidence of cell aneuploidy due to abnormal chromosomal segregation
CC (PubMed:17611414). Show abnormal formation and localization of
CC heterochromatin (PubMed:21854770). {ECO:0000269|PubMed:17611414,
CC ECO:0000269|PubMed:21854770}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX11/CHL1 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH79656.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AC119957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC079656; AAH79656.1; ALT_SEQ; mRNA.
DR CCDS; CCDS89137.1; -.
DR RefSeq; NP_001003919.1; NM_001003919.2.
DR RefSeq; NP_001335221.1; NM_001348292.1.
DR RefSeq; XP_006524471.1; XM_006524408.3.
DR RefSeq; XP_006524472.1; XM_006524409.3.
DR AlphaFoldDB; Q6AXC6; -.
DR STRING; 10090.ENSMUSP00000130440; -.
DR iPTMnet; Q6AXC6; -.
DR PhosphoSitePlus; Q6AXC6; -.
DR EPD; Q6AXC6; -.
DR PaxDb; Q6AXC6; -.
DR PeptideAtlas; Q6AXC6; -.
DR PRIDE; Q6AXC6; -.
DR ProteomicsDB; 279848; -.
DR ProteomicsDB; 348808; -.
DR Antibodypedia; 24573; 235 antibodies from 25 providers.
DR DNASU; 320209; -.
DR Ensembl; ENSMUST00000224497; ENSMUSP00000153436; ENSMUSG00000035842.
DR GeneID; 320209; -.
DR KEGG; mmu:320209; -.
DR UCSC; uc008dha.1; mouse.
DR CTD; 1663; -.
DR MGI; MGI:2443590; Ddx11.
DR VEuPathDB; HostDB:ENSMUSG00000035842; -.
DR eggNOG; KOG1133; Eukaryota.
DR GeneTree; ENSGT00950000182970; -.
DR HOGENOM; CLU_006515_2_1_1; -.
DR InParanoid; Q6AXC6; -.
DR OrthoDB; 186062at2759; -.
DR PhylomeDB; Q6AXC6; -.
DR TreeFam; TF300435; -.
DR BioGRID-ORCS; 320209; 27 hits in 108 CRISPR screens.
DR ChiTaRS; Ddx11; mouse.
DR PRO; PR:Q6AXC6; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6AXC6; protein.
DR Bgee; ENSMUSG00000035842; Expressed in primary oocyte and 143 other tissues.
DR ExpressionAtlas; Q6AXC6; baseline and differential.
DR Genevisible; Q6AXC6; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:MGI.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; ISO:MGI.
DR GO; GO:0003688; F:DNA replication origin binding; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0051880; F:G-quadruplex DNA binding; ISS:UniProtKB.
DR GO; GO:0004386; F:helicase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0045142; F:triplex DNA binding; ISS:UniProtKB.
DR GO; GO:1904976; P:cellular response to bleomycin; ISS:UniProtKB.
DR GO; GO:0072719; P:cellular response to cisplatin; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0034085; P:establishment of sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; ISS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
DR GO; GO:1990700; P:nucleolar chromatin organization; ISS:UniProtKB.
DR GO; GO:0035563; P:positive regulation of chromatin binding; ISS:UniProtKB.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; ISS:UniProtKB.
DR GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0045876; P:positive regulation of sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISS:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR028331; CHL1/DDX11.
DR InterPro; IPR010614; DEAD_2.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR PANTHER; PTHR11472; PTHR11472; 1.
DR PANTHER; PTHR11472:SF41; PTHR11472:SF41; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00604; rad3; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Activator; ATP-binding; Cytoplasm; Cytoskeleton;
KW Developmental protein; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..906
FT /note="ATP-dependent DNA helicase DDX11"
FT /id="PRO_0000055137"
FT DOMAIN 9..442
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 78..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 390..393
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 83..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 265
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FC9"
SQ SEQUENCE 906 AA; 101968 MW; E08FD46022A60B89 CRC64;
MADENQEIGG IHFPFPFPPY PIQKDFMAEL YKVLEGGKIG IFESPTGTGK SLSLICGALS
WLRDFEKKKL QAEALLLAPG SGPPSSEKNS LLTSSSCQEP TDTPRPAGEP DWVTEFVQKK
EERDLVERLR EEQVRRRKRE ERLKEVCQDG RLRFAAKRTK HEEEETEALL RLSREMLDAG
TGPEQLEQLE CGEEHLVLAE YESDEERRGS RVDEAEDDLE EEHITKIYYC SRTHSQLAQF
VREVLKSPFG KETRLVSLGS RQTLCVNEDV KNLGSVQLMN DRCVDMQRSK REKNGTGEDK
PKRKRQKIQT SCPFYNHEQM ELLRDEILLE VKDMEQLVAL GKEARACPYY GSRFAIPAAQ
LVVLPYPMLL HAATRQAAGI RLQGQVVIID EAHNLIDTIT NIHSTEVNGS QLCQAHSQLL
QYMERYRKRL KAKNLMYIKQ ILYLLEKFVA VLGGNVKQNP TTQSLSQTGS ELKSINDFLF
QSQVDNINLF KVQRYLEKSM LSRKLFGFTE CFGVVLPSLS DSQENRGLAG FQQFLKSLQS
GPTEDSPEEG QAVALRPASP LMHIEAFLAA LTTANQDGRV IVNRQGSVGQ SSLKFLLLNP
AVHFAQVVKE CRAVVIAGGT MQPMSDFREQ LLACSGVEAG RVVEFSCGHV IPPDNILPLI
ICSGPSNQQL EFTYQRRELP QMVEETGRIL CNLCNVVPGG VVCFLPSYEY LRQVHAHWDK
TGLLTRLSVR KKIFQEPKRA SQVEQVLMAY SKCIMSCSHS EGHLTGALLL SVVGGKMSEG
INFSDDLGRC VVMVGMPYPN IKSPELQEKM AYLNQTLPRT QGQPLPGTVL IENLCMKAIN
QSIGRAIRHQ RDFASIVLLD HRYARPSILA KLPAWIRDRV EVKATFGPAF AAVRKFHREK
SHPSLV
