ID DDX11_HUMAN Reviewed; 970 AA.
AC Q96FC9; Q13333; Q86VQ4; Q86W62; Q92498; Q92770; Q92998; Q92999;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 12-APR-2017, entry version 140.
DE RecName: Full=ATP-dependent DNA helicase DDX11 {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000269|PubMed:10648783, ECO:0000269|PubMed:18499658, ECO:0000269|PubMed:22102414, ECO:0000269|PubMed:26089203, ECO:0000269|PubMed:27477908};
DE AltName: Full=CHL1-related protein 1 {ECO:0000303|PubMed:9013641};
DE Short=hCHLR1 {ECO:0000303|PubMed:9013641};
DE AltName: Full=DEAD/H-box protein 11 {ECO:0000312|HGNC:HGNC:2736};
DE AltName: Full=Keratinocyte growth factor-regulated gene 2 protein {ECO:0000303|PubMed:8798685};
DE Short=KRG-2 {ECO:0000303|PubMed:8798685};
GN Name=DDX11 {ECO:0000312|HGNC:HGNC:2736};
GN Synonyms=CHL1, CHLR1 {ECO:0000303|PubMed:9013641},
GN KRG2 {ECO:0000303|PubMed:8798685};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, INDUCTION,
RP AND VARIANT SER-39.
RC TISSUE=Keratinocyte;
RX PubMed=8798685; DOI=10.1074/jbc.271.40.24337;
RA Frank S., Werner S.;
RT "The human homologue of the yeast CHL1 gene is a novel keratinocyte
RT growth factor regulated gene.";
RL J. Biol. Chem. 271:24337-24340(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND VARIANT GLU-567.
RX PubMed=9013641; DOI=10.1074/jbc.272.6.3823;
RA Amann J., Kidd V.J., Lahti J.M.;
RT "Characterization of putative human homologues of the yeast chromosome
RT transmission fidelity gene, CHL1.";
RL J. Biol. Chem. 272:3823-3832(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), AND VARIANTS GLU-567
RP AND MET-575.
RA Ouellette M.M., Wright W.E., Shay J.W.;
RT "Isolation and characterization of the human homologue of the yeast
RT CHL1 gene.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Testis, and Uterus;
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 [5]
RP CATALYTIC ACTIVITY, ENZYME ACTIVITY, FUNCTION, AND MUTAGENESIS OF
RP LYS-50.
RX PubMed=10648783; DOI=10.1093/nar/28.4.917;
RA Hirota Y., Lahti J.M.;
RT "Characterization of the enzymatic activity of hChlR1, a novel human
RT DNA helicase.";
RL Nucleic Acids Res. 28:917-924(2000).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH A COHESIN COMPLEX,
RP AND INTERACTION WITH RAD21; SMC1 PROTEINS AND SMC3.
RX PubMed=17105772; DOI=10.1242/jcs.03262;
RA Parish J.L., Rosa J., Wang X., Lahti J.M., Doxsey S.J., Androphy E.J.;
RT "The DNA helicase ChlR1 is required for sister chromatid cohesion in
RT mammalian cells.";
RL J. Cell Sci. 119:4857-4865(2006).
RN [7]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH BOVINE PAPILLOMAVIRUS
RP TYPE 1 REGULATORY PROTEIN E2 (MICROBIAL INFECTION), AND SUBCELLULAR
RP LOCATION (MICROBIAL INFECTION).
RX PubMed=17189189; DOI=10.1016/j.molcel.2006.11.005;
RA Parish J.L., Bean A.M., Park R.B., Androphy E.J.;
RT "ChlR1 is required for loading papillomavirus E2 onto mitotic
RT chromosomes and viral genome maintenance.";
RL Mol. Cell 24:867-876(2006).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, ASSOCIATES WITH THE
RP CTF18-RFC COMPLEX, INTERACTION WITH CHTF18; DSCC1; FEN1; PCNA AND
RP RFC2, AND MUTAGENESIS OF LYS-50.
RX PubMed=18499658; DOI=10.1074/jbc.M802696200;
RA Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S.,
RA Hurwitz J.;
RT "Studies with the human cohesin establishment factor, ChlR1.
RT Association of ChlR1 with Ctf18-RFC and Fen1.";
RL J. Biol. Chem. 283:20925-20936(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP INVOLVEMENT IN WBRS.
RX PubMed=20137776; DOI=10.1016/j.ajhg.2010.01.008;
RA van der Lelij P., Chrzanowska K.H., Godthelp B.C., Rooimans M.A.,
RA Oostra A.B., Stumm M., Zdzienicka M.Z., Joenje H., de Winter J.P.;
RT "Warsaw breakage syndrome, a cohesinopathy associated with mutations
RT in the XPD helicase family member DDX11/ChlR1.";
RL Am. J. Hum. Genet. 86:262-266(2010).
RN [11]
RP FUNCTION, AND INTERACTION WITH TIMELESS.
RX PubMed=20124417; DOI=10.1242/jcs.057984;
RA Leman A.R., Noguchi C., Lee C.Y., Noguchi E.;
RT "Human Timeless and Tipin stabilize replication forks and facilitate
RT sister-chromatid cohesion.";
RL J. Cell Sci. 123:660-670(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION.
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).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-50.
RX PubMed=22102414; DOI=10.1074/jbc.M111.276022;
RA Wu Y., Sommers J.A., Khan I., de Winter J.P., Brosh R.M. Jr.;
RT "Biochemical characterization of Warsaw breakage syndrome helicase.";
RL J. Biol. Chem. 287:1007-1021(2012).
RN [15]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=23116066; DOI=10.1186/1476-4598-11-82;
RA Bhattacharya C., Wang X., Becker D.;
RT "The DEAD/DEAH box helicase, DDX11, is essential for the survival of
RT advanced melanomas.";
RL Mol. Cancer 11:82-82(2012).
RN [16]
RP FUNCTION.
RX PubMed=23797032; DOI=10.1016/j.yexcr.2013.06.005;
RA Shah N., Inoue A., Woo Lee S., Beishline K., Lahti J.M., Noguchi E.;
RT "Roles of ChlR1 DNA helicase in replication recovery from DNA
RT damage.";
RL Exp. Cell Res. 319:2244-2253(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH POLR1A AND UBTF,
RP SUBCELLULAR LOCATION, INDUCTION, VARIANT WBRS GLN-263, AND
RP CHARACTERIZATION OF VARIANT WBRS GLN-263.
RX PubMed=26089203; DOI=10.1093/hmg/ddv213;
RA Sun X., Chen H., Deng Z., Hu B., Luo H., Zeng X., Han L., Cai G.,
RA Ma L.;
RT "The Warsaw breakage syndrome-related protein DDX11 is required for
RT ribosomal RNA synthesis and embryonic development.";
RL Hum. Mol. Genet. 24:4901-4915(2015).
RN [19]
RP FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, CHROMATIN-BINDING,
RP AND RNA-BINDING.
RX PubMed=27477908; DOI=10.1016/j.molcel.2016.06.031;
RA Marchese F.P., Grossi E., Marin-Bejar O., Bharti S.K., Raimondi I.,
RA Gonzalez J., Martinez-Herrera D.J., Athie A., Amadoz A.,
RA Brosh R.M. Jr., Huarte M.;
RT "A Long Noncoding RNA Regulates Sister Chromatid Cohesion.";
RL Mol. Cell 63:397-407(2016).
RN [20]
RP FUNCTION, AND INTERACTION WITH TIMELESS.
RX PubMed=26503245; DOI=10.1093/nar/gkv1112;
RA Cali F., Bharti S.K., Di Perna R., Brosh R.M. Jr., Pisani F.M.;
RT "Tim/Timeless, a member of the replication fork protection complex,
RT operates with the Warsaw breakage syndrome DNA helicase DDX11 in the
RT same fork recovery pathway.";
RL Nucleic Acids Res. 44:705-717(2016).
RN [21]
RP VARIANT WBRS GLN-263, AND CHARACTERIZATION OF VARIANT WBRS GLN-263.
RX PubMed=23033317; DOI=10.1002/humu.22226;
RA Capo-Chichi J.M., Bharti S.K., Sommers J.A., Yammine T., Chouery E.,
RA Patry L., Rouleau G.A., Samuels M.E., Hamdan F.F., Michaud J.L.,
RA Brosh R.M. Jr., Megarbane A., Kibar Z.;
RT "Identification and biochemical characterization of a novel mutation
RT in DDX11 causing warsaw breakage syndrome.";
RL Hum. Mutat. 34:103-107(2013).
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 (PubMed:10648783,
CC PubMed:21854770, PubMed:23797032, PubMed:26089203,
CC PubMed:26503245). 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-
CC stranded gapped DNA substrates of a partial duplex DNA structure
CC for helicase loading and translocation along DNA in a 5' to 3'
CC direction (PubMed:18499658, PubMed:22102414). The helicase
CC 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
CC (RPA) or the cohesion CTF18-replication factor C (Ctf18-RFC)
CC complex activities (PubMed:18499658). Shows also ATPase- and
CC helicase activities on substrates that mimic key DNA intermediates
CC of replication, repair and homologous recombination reactions,
CC including forked duplex, anti-parallel G-quadruplex and three-
CC stranded D-loop DNA molecules (PubMed:22102414, PubMed:26503245).
CC Plays a role in DNA double-strand break (DSB) repair at the DNA
CC replication fork during DNA replication recovery from DNA damage
CC (PubMed:23797032). Recruited with TIMELESS factor upon DNA-
CC replication stress response at DNA replication fork to preserve
CC replication fork progression, and hence ensure DNA replication
CC fidelity (PubMed:26503245). Cooperates also with TIMELESS factor
CC during DNA replication to regulate proper sister chromatid
CC cohesion and mitotic chromosome segregation (PubMed:17105772,
CC PubMed:18499658, PubMed:20124417, PubMed:23116066,
CC PubMed:23797032). Stimulates 5'-single-stranded DNA flap
CC endonuclease activity of FEN1 in an ATP- and helicase-independent
CC manner; and hence it may contribute in Okazaki fragment processing
CC at DNA replication fork during lagging strand DNA synthesis
CC (PubMed:18499658). Its ability to function at DNA replication fork
CC is modulated by its binding to long non-coding RNA (lncRNA)
CC cohesion regulator non-coding RNA DDX11-AS1/CONCR, which is able
CC to increase both DDX11 ATPase activity and binding to DNA
CC replicating regions (PubMed:27477908). Plays also a role in
CC heterochromatin organization (PubMed:21854770). Involved in rRNA
CC transcription activation through binding to active hypomethylated
CC rDNA gene loci by recruiting UBTF and the RNA polymerase Pol I
CC transcriptional machinery (PubMed:26089203). Plays a role in
CC embryonic development and prevention of aneuploidy (By
CC similarity). Involved in melanoma cell proliferation and survival
CC (PubMed:23116066). Associates with chromatin at DNA replication
CC fork regions (PubMed:27477908). Binds to single- and double-
CC stranded DNAs (PubMed:9013641, PubMed:18499658, PubMed:22102414).
CC {ECO:0000250|UniProtKB:Q6AXC6, ECO:0000269|PubMed:10648783,
CC ECO:0000269|PubMed:17105772, ECO:0000269|PubMed:18499658,
CC ECO:0000269|PubMed:20124417, ECO:0000269|PubMed:21854770,
CC ECO:0000269|PubMed:22102414, ECO:0000269|PubMed:23116066,
CC ECO:0000269|PubMed:23797032, ECO:0000269|PubMed:26089203,
CC ECO:0000269|PubMed:26503245, ECO:0000269|PubMed:27477908}.
CC -!- FUNCTION: (Microbial infection) Required for bovine papillomavirus
CC type 1 regulatory protein E2 loading onto mitotic chromosomes
CC during DNA replication for the viral genome to be maintained and
CC segragated. {ECO:0000269|PubMed:17189189}.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC {ECO:0000269|PubMed:10648783, ECO:0000269|PubMed:18499658,
CC ECO:0000269|PubMed:22102414, ECO:0000269|PubMed:26089203,
CC ECO:0000269|PubMed:27477908}.
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 -!- ENZYME REGULATION: ATPase activity is stimulated by high magnesium
CC salt levels (up to a 0.1 M), and potassium salts (glutamate,
CC chloride or acetate) are more effective than the corresponding
CC sodium salts (PubMed:10648783, PubMed:18499658). ATPase activity
CC is enhanced by the long non-coding RNA (lncRNA) cohesion regulator
CC noncoding RNA (CONCR) (PubMed:27477908). Double-stranded DNA
CC helicase activity is maximal with magnesium ions at low
CC concentrations (0.5-1 mM) whereas is markedly inhibited at higher
CC levels (5 mM and above) (PubMed:10648783, PubMed:18499658).
CC Double-stranded DNA helicase activity is stimulated by 25-50 mM
CC potassium acetate, stimulated to a lesser extent by 25 mM of
CC ammonium acetate, and markedly inhibited by sodium acetate
CC (PubMed:18499658). {ECO:0000269|PubMed:10648783,
CC ECO:0000269|PubMed:18499658, ECO:0000269|PubMed:27477908}.
CC -!- SUBUNIT: Associates with the CTF18-RFC complex (PubMed:18499658).
CC Associates with a cohesin complex composed of RAD21, SMC1 proteins
CC and SMC3 (PubMed:17105772). Interacts with CHTF18
CC (PubMed:18499658). Interacts with DSCC1 (PubMed:18499658).
CC Interacts with FEN1; this interaction is direct and increases flap
CC endonuclease activity of FEN1 (PubMed:18499658). Interacts with
CC PCNA (PubMed:18499658). Interacts with POLR1A and UBTF
CC (PubMed:26089203). Interacts with RAD21, SMC1 proteins and SMC3
CC (PubMed:17105772). Interacts with RFC2 (PubMed:18499658).
CC Interacts with TIMELESS; this interaction increases recruitment of
CC both proteins onto chromatin in response to replication stress
CC induction by hydroxyurea (PubMed:20124417, PubMed:26503245).
CC {ECO:0000269|PubMed:17105772, ECO:0000269|PubMed:18499658,
CC ECO:0000269|PubMed:20124417, ECO:0000269|PubMed:26089203,
CC ECO:0000269|PubMed:26503245}.
CC -!- SUBUNIT: (Microbial infection) Interacts with bovine
CC papillomavirus type 1 regulatory protein E2; this interaction
CC stimulates the recruitment of E2 onto mitotic chromosomes.
CC {ECO:0000269|PubMed:17189189}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17105772}.
CC Nucleus, nucleolus {ECO:0000269|PubMed:17105772,
CC ECO:0000269|PubMed:26089203, ECO:0000269|PubMed:9013641}.
CC Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:17105772}. Midbody
CC {ECO:0000269|PubMed:17105772}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:17105772}. 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) (PubMed:17105772). In
CC interphase, colocalizes with nucleolin in the nucleolus
CC (PubMed:26089203). {ECO:0000269|PubMed:17105772,
CC ECO:0000269|PubMed:26089203}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:17189189}.
CC Note=(Microbial infection) Colocalizes with bovine papillomavirus
CC type 1 regulatory protein E2 on mitotic chromosomes at early
CC stages of mitosis. {ECO:0000269|PubMed:17189189}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96FC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96FC9-2; Sequence=VSP_016864, VSP_016865;
CC Name=3;
CC IsoId=Q96FC9-3; Sequence=VSP_016860, VSP_016864, VSP_016865;
CC Name=4;
CC IsoId=Q96FC9-4; Sequence=VSP_016863, VSP_016864, VSP_016865;
CC Name=5;
CC IsoId=Q96FC9-5; Sequence=VSP_016861, VSP_016862;
CC -!- TISSUE SPECIFICITY: Expressed in melanoma cells. Not detected in
CC epidermal melanocytes of normal skin (at protein level)
CC (PubMed:23116066). Highly expressed in spleen, B-cells, thymus,
CC testis, ovary, small intestine and pancreas (PubMed:9013641). Very
CC low expression seen in brain (PubMed:9013641). Expressed in
CC dividing cells and/or cells undergoing high levels of
CC recombination (PubMed:9013641). No expression detected in cells
CC signaled to terminally differentiate (PubMed:9013641). Expressed
CC weakly in keratinocytes (PubMed:8798685).
CC {ECO:0000269|PubMed:23116066, ECO:0000269|PubMed:8798685,
CC ECO:0000269|PubMed:9013641}.
CC -!- INDUCTION: Up-regulated by serum (at protein level)
CC (PubMed:26089203). Up-regulated by fibroblast growth factor FGF7
CC (PubMed:8798685). Expressed in keratinocyte growth factor-
CC stimulated cells but not in EGF and IL1-beta-treated keratinocytes
CC (PubMed:8798685). Up-regulated with progression from noninvasive
CC to invasive melanoma (PubMed:23116066).
CC {ECO:0000269|PubMed:23116066, ECO:0000269|PubMed:26089203,
CC ECO:0000269|PubMed:8798685}.
CC -!- DISEASE: Warsaw breakage syndrome (WBRS) [MIM:613398]: A syndrome
CC characterized by severe microcephaly, pre- and postnatal growth
CC retardation, facial dysmorphism and abnormal skin pigmentation.
CC Additional features include high arched palate, coloboma of the
CC right optic disk, deafness, ventricular septal defect, toes and
CC fingers abnormalities. At cellular level, drug-induced chromosomal
CC breakage, a feature of Fanconi anemia, and sister chromatid
CC cohesion defects, a feature of Roberts syndrome, coexist.
CC {ECO:0000269|PubMed:20137776, ECO:0000269|PubMed:23033317,
CC ECO:0000269|PubMed:26089203}. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC subfamily. DDX11/CHL1 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA67895.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC Sequence=CAA67895.1; Type=Frameshift; Positions=644, 648; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=DEAD/H (Asp-Glu-Ala-Asp/His) box helicase 11
CC (DDX11); Note=Leiden Open Variation Database (LOVD);
CC URL="http://www.lovd.nl/DDX11";
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DR EMBL; X99583; CAA67895.1; ALT_SEQ; mRNA.
DR EMBL; U33833; AAB06962.1; -; mRNA.
DR EMBL; U75967; AAB18749.1; -; mRNA.
DR EMBL; U75968; AAB18750.1; -; mRNA.
DR EMBL; BC050069; AAH50069.1; -; mRNA.
DR EMBL; BC050522; AAH50522.1; -; mRNA.
DR CCDS; CCDS41767.1; -. [Q96FC9-2]
DR CCDS; CCDS44856.1; -. [Q96FC9-1]
DR CCDS; CCDS58224.1; -. [Q96FC9-3]
DR CCDS; CCDS8721.1; -. [Q96FC9-4]
DR PIR; G02071; G02071.
DR RefSeq; NP_001244073.1; NM_001257144.1. [Q96FC9-1]
DR RefSeq; NP_001244074.1; NM_001257145.1. [Q96FC9-3]
DR RefSeq; NP_004390.3; NM_004399.2. [Q96FC9-4]
DR RefSeq; NP_689651.1; NM_152438.1. [Q96FC9-1]
DR RefSeq; XP_016874421.1; XM_017018932.1. [Q96FC9-2]
DR UniGene; Hs.443960; -.
DR ProteinModelPortal; Q96FC9; -.
DR BioGrid; 108028; 30.
DR IntAct; Q96FC9; 5.
DR MINT; MINT-1371028; -.
DR STRING; 9606.ENSP00000384703; -.
DR iPTMnet; Q96FC9; -.
DR PhosphoSitePlus; Q96FC9; -.
DR BioMuta; DDX11; -.
DR DMDM; 74731686; -.
DR EPD; Q96FC9; -.
DR MaxQB; Q96FC9; -.
DR PaxDb; Q96FC9; -.
DR PeptideAtlas; Q96FC9; -.
DR PRIDE; Q96FC9; -.
DR DNASU; 1663; -.
DR Ensembl; ENST00000228264; ENSP00000228264; ENSG00000013573. [Q96FC9-3]
DR Ensembl; ENST00000350437; ENSP00000309965; ENSG00000013573. [Q96FC9-4]
DR Ensembl; ENST00000435753; ENSP00000406799; ENSG00000013573. [Q96FC9-5]
DR Ensembl; ENST00000542838; ENSP00000443426; ENSG00000013573. [Q96FC9-2]
DR Ensembl; ENST00000545668; ENSP00000440402; ENSG00000013573. [Q96FC9-1]
DR GeneID; 1663; -.
DR KEGG; hsa:1663; -.
DR UCSC; uc001rjr.2; human. [Q96FC9-1]
DR CTD; 1663; -.
DR DisGeNET; 1663; -.
DR GeneCards; DDX11; -.
DR HGNC; HGNC:2736; DDX11.
DR HPA; HPA065197; -.
DR MalaCards; DDX11; -.
DR MIM; 601150; gene.
DR MIM; 613398; phenotype.
DR neXtProt; NX_Q96FC9; -.
DR OpenTargets; ENSG00000013573; -.
DR Orphanet; 280558; Warsaw breakage syndrome.
DR PharmGKB; PA27201; -.
DR eggNOG; KOG1133; Eukaryota.
DR eggNOG; COG1199; LUCA.
DR GeneTree; ENSGT00530000063199; -.
DR HOVERGEN; HBG058884; -.
DR InParanoid; Q96FC9; -.
DR KO; K11273; -.
DR OMA; NLCQVIP; -.
DR OrthoDB; EOG091G034C; -.
DR PhylomeDB; Q96FC9; -.
DR TreeFam; TF300435; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR GeneWiki; DDX11; -.
DR GenomeRNAi; 1663; -.
DR PRO; PR:Q96FC9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR Bgee; ENSG00000013573; -.
DR CleanEx; HS_CHL1; -.
DR CleanEx; HS_DDX11; -.
DR ExpressionAtlas; Q96FC9; baseline and differential.
DR Genevisible; Q96FC9; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0000922; C:spindle pole; IDA: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; IDA:UniProtKB.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003688; F:DNA replication origin binding; IMP:UniProtKB.
DR GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IDA:UniProtKB.
DR GO; GO:0004386; F:helicase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008186; F:RNA-dependent ATPase activity; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0045142; F:triplex DNA binding; IDA:UniProtKB.
DR GO; GO:1904976; P:cellular response to bleomycin; IMP:UniProtKB.
DR GO; GO:0072719; P:cellular response to cisplatin; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0072711; P:cellular response to hydroxyurea; IMP:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IDA:UniProtKB.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
DR GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR GO; GO:0032091; P:negative regulation of protein binding; IMP:UniProtKB.
DR GO; GO:1990700; P:nucleolar chromatin organization; IMP:UniProtKB.
DR GO; GO:0035563; P:positive regulation of chromatin binding; IDA:UniProtKB.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IMP:UniProtKB.
DR GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0045876; P:positive regulation of sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:1901838; P:positive regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter; IMP:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; IMP:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral process; 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; Alternative splicing; ATP-binding; Chromosome;
KW Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein;
KW Disease mutation; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Helicase; Host-virus interaction; Hydrolase; Iron;
KW Iron-sulfur; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; RNA-binding;
KW Transcription; Transcription regulation.
FT CHAIN 1 970 ATP-dependent DNA helicase DDX11.
FT /FTId=PRO_0000055136.
FT DOMAIN 9 445 Helicase ATP-binding.
FT {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT NP_BIND 44 51 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00541}.
FT MOTIF 393 396 DEAH box.
FT COMPBIAS 163 224 Glu-rich.
FT METAL 267 267 Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT METAL 285 285 Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT METAL 315 315 Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT METAL 350 350 Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT MOD_RES 262 262 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT VAR_SEQ 1 26 Missing (in isoform 3).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_016860.
FT VAR_SEQ 214 288 VDEDEDDLEEEHITKIYYCSRTHSQLAQFVHEVKKSPFGKD
FT VRLVSLGSRQNLCVNEDVKSLGSVQLINDRCVDM -> APS
FT DATSSRHPPDASFPAALNFLQRTRPSSVLSEDLLMQRAVAK
FT HPALLPWQMSSSPLRPGSEWMRMRMTWRKNT (in
FT isoform 5). {ECO:0000303|Ref.3}.
FT /FTId=VSP_016861.
FT VAR_SEQ 289 970 Missing (in isoform 5).
FT {ECO:0000303|Ref.3}.
FT /FTId=VSP_016862.
FT VAR_SEQ 685 734 Missing (in isoform 4).
FT {ECO:0000303|PubMed:8798685}.
FT /FTId=VSP_016863.
FT VAR_SEQ 820 906 SPRPGTPREGSGGEPVHEGRQPVHRQGHQAPEGFCQRSAPG
FT PAICPAPCPGQAAGLDPSPCGGQSYLWPRHCCCAEVSPGEV
FT GLFLM -> PRAPGQAPPGKALVENLCMKAVNQSIGRAIRH
FT QKDFASVVLLDQRYARPPVLAKLPAWIRARVEVKATFGPAI
FT AAVQKFHREKSASS (in isoform 2, isoform 3
FT and isoform 4).
FT {ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8798685,
FT ECO:0000303|PubMed:9013641,
FT ECO:0000303|Ref.3}.
FT /FTId=VSP_016864.
FT VAR_SEQ 907 970 Missing (in isoform 2, isoform 3 and
FT isoform 4). {ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8798685,
FT ECO:0000303|PubMed:9013641,
FT ECO:0000303|Ref.3}.
FT /FTId=VSP_016865.
FT VARIANT 39 39 I -> S (in dbSNP:rs1046454).
FT {ECO:0000269|PubMed:8798685}.
FT /FTId=VAR_024808.
FT VARIANT 263 263 R -> Q (in WBRS; impairs the helicase
FT activity by perturbing its DNA binding
FT and DNA-dependent ATPase activity;
FT reduces binding to rDNA promoter and
FT promotion of rDNA transcription;
FT dbSNP:rs201968272).
FT {ECO:0000269|PubMed:23033317,
FT ECO:0000269|PubMed:26089203}.
FT /FTId=VAR_069099.
FT VARIANT 567 567 Q -> E (in dbSNP:rs2075322).
FT {ECO:0000269|PubMed:9013641,
FT ECO:0000269|Ref.3}.
FT /FTId=VAR_024809.
FT VARIANT 575 575 T -> M (in dbSNP:rs17857386).
FT {ECO:0000269|Ref.3}.
FT /FTId=VAR_024810.
FT VARIANT 856 856 R -> H (in dbSNP:rs1046457).
FT /FTId=VAR_052175.
FT VARIANT 864 864 C -> R (in dbSNP:rs3893679).
FT /FTId=VAR_052176.
FT VARIANT 951 951 C -> R (in dbSNP:rs1046458).
FT /FTId=VAR_052177.
FT VARIANT 966 966 W -> C (in dbSNP:rs14330).
FT /FTId=VAR_052178.
FT MUTAGEN 50 50 K->R: Loss of both DNA-dependent ATPase
FT and ATP-dependent helicase activities.
FT {ECO:0000269|PubMed:10648783,
FT ECO:0000269|PubMed:18499658,
FT ECO:0000269|PubMed:22102414}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 9 445 iprf:HELICASE_ATP_BIND_2 [T]
FT MYHIT 231 415 ipfam:DEAD_2 [T]
FT MYHIT 710 859 ismart:HELICc2 [T]
FT MYHIT 11 437 ismart:DEXDc2 [T]
FT MYHIT 692 820 ipfam:Helicase_C_2 [T]
SQ SEQUENCE 970 AA; 108313 MW; 5BF49FE74E912B48 CRC64;
MANETQKVGA IHFPFPFTPY SIQEDFMAEL YRVLEAGKIG IFESPTGTGK SLSLICGALS
WLRDFEQKKR EEEARLLETG TGPLHDEKDE SLCLSSSCEG AAGTPRPAGE PAWVTQFVQK
KEERDLVDRL KAEQARRKQR EERLQQLQHR VQLKYAAKRL RQEEEERENL LRLSREMLET
GPEAERLEQL ESGEEELVLA EYESDEEKKV ASRVDEDEDD LEEEHITKIY YCSRTHSQLA
QFVHEVKKSP FGKDVRLVSL GSRQNLCVNE DVKSLGSVQL INDRCVDMQR SRHEKKKGAE
EEKPKRRRQE KQAACPFYNH EQMGLLRDEA LAEVKDMEQL LALGKEARAC PYYGSRLAIP
AAQLVVLPYQ MLLHAATRQA AGIRLQDQVV IIDEAHNLID TITGMHSVEV SGSQLCQAHS
QLLQYVERYG KRLKAKNLMY LKQILYLLEK FVAVLGGNIK QNPNTQSLSQ TGTELKTIND
FLFQSQIDNI NLFKVQRYCE KSMISRKLFG FTERYGAVFS SREQPKLAGF QQFLQSLQPR
TTEALAAPAD ESQASTLRPA SPLMHIQGFL AALTTANQDG RVILSRQGSL SQSTLKFLLL
NPAVHFAQVV KECRAVVIAG GTMQPVSDFR QQLLACAGVE AERVVEFSCG HVIPPDNILP
LVICSGISNQ PLEFTFQKRE LPQMMDEVGR ILCNLCGVVP GGVVCFFPSY EYLRQVHAHW
EKGGLLGRLA ARKKIFQEPK SAHQVEQVLL AYSRCIQACG QERGQVTGAL LLSVVGGKMS
EGINFSDNLG RCVVMVGMPF PNIRSAELQE KMAYLDQTLS PRPGTPREGS GGEPVHEGRQ
PVHRQGHQAP EGFCQRSAPG PAICPAPCPG QAAGLDPSPC GGQSYLWPRH CCCAEVSPGE
VGLFLMGNHT TAWRRALPLS CPLETVFVVG VVCGDPVTKV KPRRRVWSPE CCQDPGTGVS
SRRRKWGNPE
//
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