Entry euk:DDX11_MOUSE

ID   DDX11_MOUSE             Reviewed;         880 AA.
AC   Q6AXC6;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   10-MAY-2017, entry version 113.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
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.,
RA   Kidd V.J., Lahti J.M.;
RT   "Loss of ChlR1 helicase in mouse causes lethality due to the
RT   accumulation of aneuploid cells generated by cohesion defects and
RT   placental malformation.";
RL   Cell Cycle 6:1646-1654(2007).
RN   [3]
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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
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
CC       DNA replication, DNA repair and heterochromatin organization as
CC       well as in ribosomal RNA synthesis. Its double-stranded DNA
CC       helicase activity requires either a minimal 5'-single-stranded
CC       tail length of approximately 15 nt (flap substrates) or 10 nt
CC       length single-stranded gapped DNA substrates of a partial duplex
CC       DNA structure for helicase loading and translocation along DNA in
CC       a 5' to 3' direction. The helicase activity is capable of
CC       displacing duplex regions up to 100 bp, which can be extended up
CC       to 500 bp by the replication protein A (RPA) or the cohesion
CC       CTF18-replication factor C (Ctf18-RFC) complex activities. Shows
CC       also ATPase- and helicase activities on substrates that mimic key
CC       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
CC       in DNA double-strand break (DSB) repair at the DNA replication
CC       fork during DNA replication recovery from DNA damage. Recruited
CC       with TIMELESS factor upon DNA-replication stress response at DNA
CC       replication fork to preserve replication fork progression, and
CC       hence ensure DNA replication fidelity (By similarity). Cooperates
CC       also with TIMELESS factor during DNA replication to regulate
CC       proper sister chromatid cohesion and mitotic chromosome
CC       segregation (PubMed:17611414). Stimulates 5'-single-stranded DNA
CC       flap endonuclease activity of FEN1 in an ATP- and helicase-
CC       independent manner; and hence it may contribute in Okazaki
CC       fragment processing at DNA replication fork during lagging strand
CC       DNA synthesis. Its ability to function at DNA replication fork is
CC       modulated by its binding to long non-coding RNA (lncRNA) cohesion
CC       regulator non-coding RNA DDX11-AS1/CONCR, which is able to
CC       increase both DDX11 ATPase activity and binding to DNA replicating
CC       regions (By similarity). Plays also a role in heterochromatin
CC       organization (PubMed:21854770). Involved in rRNA transcription
CC       activation through binding to active hypomethylated rDNA gene loci
CC       by recruiting UBTF and the RNA polymerase Pol I transcriptional
CC       machinery (By similarity). Plays a role in embryonic development
CC       and prevention of aneuploidy (PubMed:17611414). Involved in
CC       melanoma cell proliferation and survival. Associates with
CC       chromatin at DNA replication fork regions. Binds to single- and
CC       double-stranded DNAs (By similarity).
CC       {ECO:0000250|UniProtKB:Q96FC9, ECO:0000269|PubMed:17611414,
CC       ECO:0000269|PubMed:21854770}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC       {ECO:0000250|UniProtKB:Q96FC9}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         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.
CC       Interacts with CHTF18. Interacts with DSCC1. Interacts with FEN1;
CC       this interaction is direct and increases flap endonuclease
CC       activity of FEN1. Interacts with PCNA. Interacts with POLR1A and
CC       UBTF. Interacts with RAD21, SMC1 proteins and SMC3. Interacts with
CC       RFC2. Interacts with TIMELESS; this interaction increases
CC       recruitment of both proteins onto chromatin in response to
CC       replication stress induction by hydroxyurea.
CC       {ECO:0000250|UniProtKB:Q96FC9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96FC9}.
CC       Nucleus, nucleolus {ECO:0000250|UniProtKB:Q96FC9}. Cytoplasm,
CC       cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q96FC9}. Midbody
CC       {ECO:0000250|UniProtKB:Q96FC9}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:Q96FC9}. Note=During the early stages of
CC       mitosis, localizes to condensed chromatin and is released from the
CC       chromatin with progression to metaphase. Also localizes to the
CC       spindle poles throughout mitosis and at the midbody at later
CC       stages of mitosis (metaphase to telophase). In interphase,
CC       colocalizes with nucleolin in the nucleolus.
CC       {ECO:0000250|UniProtKB:Q96FC9}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic death at 10.5 dpc
CC       (PubMed:17611414). Embryos are smaller in size, malformed and
CC       exhibit sparse cellularity in comparison to normal or heterozygous
CC       litter mates (PubMed:17611414). Show inability to form a proper
CC       embryonic placenta. Display high incidence of cell aneuploidy due
CC       to abnormal chromosomal segregation (PubMed:17611414). Show
CC       abnormal formation and localization of heterochromatin
CC       (PubMed:21854770). {ECO:0000269|PubMed:17611414,
CC       ECO:0000269|PubMed:21854770}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. DDX11/CHL1 sub-subfamily. {ECO:0000305}.
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DR   EMBL; BC079656; AAH79656.1; -; mRNA.
DR   CCDS; CCDS28945.1; -.
DR   RefSeq; NP_001003919.1; NM_001003919.2.
DR   RefSeq; NP_001335221.1; NM_001348292.1.
DR   UniGene; Mm.259605; -.
DR   ProteinModelPortal; Q6AXC6; -.
DR   STRING; 10090.ENSMUSP00000130440; -.
DR   iPTMnet; Q6AXC6; -.
DR   PhosphoSitePlus; Q6AXC6; -.
DR   EPD; Q6AXC6; -.
DR   MaxQB; Q6AXC6; -.
DR   PaxDb; Q6AXC6; -.
DR   PeptideAtlas; Q6AXC6; -.
DR   PRIDE; Q6AXC6; -.
DR   Ensembl; ENSMUST00000163605; ENSMUSP00000130440; ENSMUSG00000035842.
DR   GeneID; 320209; -.
DR   KEGG; mmu:320209; -.
DR   UCSC; uc008dha.1; mouse.
DR   CTD; 1663; -.
DR   MGI; MGI:2443590; Ddx11.
DR   eggNOG; KOG1133; Eukaryota.
DR   eggNOG; COG1199; LUCA.
DR   GeneTree; ENSGT00530000063199; -.
DR   HOGENOM; HOG000241266; -.
DR   HOVERGEN; HBG058884; -.
DR   InParanoid; Q6AXC6; -.
DR   KO; K11273; -.
DR   OMA; NLCQVIP; -.
DR   OrthoDB; EOG091G034C; -.
DR   PhylomeDB; Q6AXC6; -.
DR   TreeFam; TF300435; -.
DR   PRO; PR:Q6AXC6; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   Bgee; ENSMUSG00000035842; -.
DR   Genevisible; Q6AXC6; MM.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0031390; C:Ctf18 RFC-like complex; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0000790; C:nuclear chromatin; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003688; F:DNA replication origin binding; ISS:UniProtKB.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; 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:0008186; F:RNA-dependent ATPase activity; ISS:UniProtKB.
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:0044806; P:G-quadruplex DNA unwinding; ISS:UniProtKB.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
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 nuclear large rRNA transcript from RNA polymerase I promoter; ISS:UniProtKB.
DR   GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR   GO; GO:0007062; P:sister chromatid cohesion; ISS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR010614; DEAD_2.
DR   InterPro; IPR013020; DNA_helicase_DNA-repair_Rad3.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006554; Helicase-like_DEXD_c2.
DR   InterPro; IPR027417; P-loop_NTPase.
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; 3.
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; Complete proteome; Cytoplasm;
KW   Cytoskeleton; Developmental protein; DNA damage; DNA repair;
KW   DNA replication; DNA-binding; Helicase; Hydrolase; Iron; Iron-sulfur;
KW   Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    880       ATP-dependent DNA helicase DDX11.
FT                                /FTId=PRO_0000055137.
FT   DOMAIN        9    416       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   NP_BIND      44     51       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       364    367       DEAH box.
FT   COMPBIAS    121    196       Glu-rich.
FT   METAL       239    239       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL       257    257       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL       286    286       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL       321    321       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   MOD_RES     234    234       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96FC9}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       682    839       ismart:HELICc2 [T]
FT   MYHIT         9    416       iprf:HELICASE_ATP_BIND_2 [T]
FT   MYHIT       203    386       ipfam:DEAD_2 [T]
FT   MYHIT       664    852       ipfam:Helicase_C_2 [T]
FT   MYHIT        11    408       ismart:DEXDc2 [T]
SQ   SEQUENCE   880 AA;  98728 MW;  0A283D952B974F82 CRC64;
     MADENQEIGG IHFPFPFPPY PIQKDFMAEL YKVLEGGKIG IFESPTGTGK SLSLICGALS
     WLRDFEKKKL QAEALLLAPG SGPPSSEKNS LLTSSSCQEP TDTPRPAGEP DWVTEFVQKK
     EERDLVERLR EEQKHEEEET EALLRLSREM LDAGTGPEQL EQLECGEEHL VLAEYESDEE
     RRGSRVDEAE DDLEEEHITK IYYCSRTHSQ LAQFVREVLK SPFGKETRLV SLGSRQTLCV
     NEDVKNLGSV QLMNDRCVDM QRSKREKNGT GEDKPKRKRQ KIQTSCPFYN HEQMELLRDE
     ILLEVKDMEQ LVALGKEARA CPYYGSRFAI PAAQLVVLPY PMLLHAATRQ AAGIRLQGQV
     VIIDEAHNLI DTITNIHSTE VNGSQLCQAH SQLLQYMERY RKRLKAKNLM YIKQILYLLE
     KFVAVLGGNV KQNPTTQSLS QTGSELKSIN DFLFQSQVDN INLFKVQRYL EKSMLSRKLF
     GFTECFGVVL PSLSDSQENR GLAGFQQFLK SLQSGPTEDS PEEGQAVALR PASPLMHIEA
     FLAALTTANQ DGRVIVNRQG SVGQSSLKFL LLNPAVHFAQ VVKECRAVVI AGGTMQPMSD
     FREQLLACSG VEAGRVVEFS CGHVIPPDNI LPLIICSGPS NQQLEFTYQR RELPQMVEET
     GRILCNLCNV VPGGVVCFLP SYEYLRQVHA HWDKTGLLTR LSVRKKIFQE PKRASQVEQV
     LMAYSKCIMS CSHSEGHLTG ALLLSVVGGK MSEGINFSDD LGRCVVMVGM PYPNIKSPEL
     QEKMAYLNQT LPRTQGQPLP GTVLIENLCM KAINQSIGRA IRHQRDFASI VLLDHRYARP
     SILAKLPAWI RDRVEVKATF GPAFAAVRKF HREKSHPSLV
//