DDX11
entrez
1663
canonical
uniprot
Q96FC9
canonical
ensembl
ENSG00000013573
resolver
ensp
ENSP00000228264
resolver
ensp
ENSP00000309965
resolver
ensp
ENSP00000440402
resolver
ensp
ENSP00000443426
resolver
ensp
ENSP00000549165
resolver
ensp
ENSP00000590010
resolver
ensp
ENSP00000590011
resolver
ensp
ENSP00000590021
resolver
ensp
ENSP00000590022
resolver
ensp
ENSP00000662374
resolver
genesymbol
DDX11
resolver
genesymbol_syn
CHL1
resolver
genesymbol_syn
CHLR1
resolver
genesymbol_syn
KRG2
resolver
hgnc
HGNC:2736
resolver
uniprot
Q13333
resolver
uniprot
Q2NKM7
resolver
uniprot
Q86VQ4
resolver
uniprot
Q86W62
resolver
uniprot
Q92498
resolver
uniprot
Q92770
resolver
uniprot
Q92998
resolver
uniprot
Q92999
resolver
uniprot_entry
DDX11_HUMAN
resolver
uniprot_entry
Q2NKM7_HUMAN
resolver
uniprot_sec
Q13333
resolver
uniprot_sec
Q86VQ4
resolver
uniprot_sec
Q86W62
resolver
uniprot_sec
Q92498
resolver
uniprot_sec
Q92770
resolver
uniprot_sec
Q92998
resolver
uniprot_sec
Q92999
resolver
activity_regulation
ACTIVITY REGULATION: ATPase activity is stimulated by high magnesium salt levels (up to a 0.1 M), and potassium salts (glutamate, chloride or acetate) are more effective than the corresponding sodium salts (PubMed:10648783, PubMed:18499658). ATPase activity is enhanced by the long non-coding RNA (lncRNA) cohesion regulator non-coding RNA (CONCR) (PubMed:27477908). Double-stranded DNA helicase activity is maximal with magnesium ions at low concentrations (0.5-1 mM) whereas is markedly inhibited at higher levels (5 mM and above) (PubMed:10648783, PubMed:18499658). Double-stranded DNA helicase activity is stimulated by 25-50 mM potassium acetate, stimulated to a lesser extent by 25 mM of ammonium acetate, and markedly inhibited by sodium acetate (PubMed:18499658). {ECO:0000269|PubMed:10648783, ECO:0000269|PubMed:18499658, ECO:0000269|PubMed:27477908}.
uniprot
proteins
amino_acid_sequence
MANETQKVGAIHFPFPFTPYSIQEDFMAELYRVLEAGKIGIFESPTGTGKSLSLICGALSWLRDFEQKKREEEARLLETGTGPLHDEKDESLCLSSSCEGAAGTPRPAGEPAWVTQFVQKKEERDLVDRLKAEQARRKQREERLQQLQHRVQLKYAAKRLRQEEEERENLLRLSREMLETGPEAERLEQLESGEEELVLAEYESDEEKKVASRVDEDEDDLEEEHITKIYYCSRTHSQLAQFVHEVKKSPFGKDVRLVSLGSRQNLCVNEDVKSLGSVQLINDRCVDMQRSRHEKKKGAEEEKPKRRRQEKQAACPFYNHEQMGLLRDEALAEVKDMEQLLALGKEARACPYYGSRLAIPAAQLVVLPYQMLLHAATRQAAGIRLQDQVVIIDEAHNLIDTITGMHSVEVSGSQLCQAHSQLLQYVERYGKRLKAKNLMYLKQILYLLEKFVAVLGGNIKQNPNTQSLSQTGTELKTINDFLFQSQIDNINLFKVQRYCEKSMISRKLFGFTERYGAVFSSREQPKLAGFQQFLQSLQPRTTEALAAPADESQASTLRPASPLMHIQGFLAALTTANQDGRVILSRQGSLSQSTLKFLLLNPAVHFAQVVKECRAVVIAGGTMQPVSDFRQQLLACAGVEAERVVEFSCGHVIPPDNILPLVICSGISNQPLEFTFQKRELPQMMDEVGRILCNLCGVVPGGVVCFFPSYEYLRQVHAHWEKGGLLGRLAARKKIFQEPKSAHQVEQVLLAYSRCIQACGQERGQVTGALLLSVVGGKMSEGINFSDNLGRCVVMVGMPFPNIRSAELQEKMAYLDQTLSPRPGTPREGSGGEPVHEGRQPVHRQGHQAPEGFCQRSAPGPAICPAPCPGQAAGLDPSPCGGQSYLWPRHCCCAEVSPGEVGLFLMGNHTTAWRRALPLSCPLETVFVVGVVCGDPVTKVKPRRRVWSPECCQDPGTGVSSRRRKWGNPE
uniprot
proteins
disease_involvement
DISEASE: Warsaw breakage syndrome (WBRS) [MIM:613398]: A syndrome characterized by severe microcephaly, pre- and postnatal growth retardation, facial dysmorphism and abnormal skin pigmentation. Additional features include high arched palate, coloboma of the right optic disk, deafness, ventricular septal defect, toes and fingers abnormalities. At cellular level, drug-induced chromosomal breakage, a feature of Fanconi anemia, and sister chromatid cohesion defects, a feature of Roberts syndrome, coexist. {ECO:0000269|PubMed:20137776, ECO:0000269|PubMed:23033317, ECO:0000269|PubMed:26089203}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
5.6.2.3
uniprot
proteins
function
FUNCTION: 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 (PubMed:10648783, PubMed:21854770, PubMed:23797032, PubMed:26089203, PubMed:26503245). 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 (PubMed:10648783, PubMed:18499658, PubMed:22102414). 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 (PubMed:18499658). Also shows 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 (PubMed:22102414, PubMed:26503245). Plays a role in DNA double-strand break (DSB) repair at the DNA replication fork during DNA replication recovery from DNA damage (PubMed:23797032). Recruited with TIMELESS factor upon DNA-replication stress response at DNA replication fork to preserve replication fork progression, and hence ensure DNA replication fidelity (PubMed:26503245). Also cooperates with TIMELESS factor during DNA replication to regulate proper sister chromatid cohesion and mitotic chromosome segregation (PubMed:17105772, PubMed:18499658, PubMed:20124417, PubMed:23116066, PubMed:23797032). 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 (PubMed:18499658). 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 (PubMed:27477908). Also plays 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 (PubMed:26089203). Plays a role in embryonic development and prevention of aneuploidy (By similarity). Involved in melanoma cell proliferation and survival (PubMed:23116066). Associates with chromatin at DNA replication fork regions (PubMed:27477908). Binds to single- and double-stranded DNAs (PubMed:18499658, PubMed:22102414, PubMed:9013641). {ECO:0000250|UniProtKB:Q6AXC6, ECO:0000269|PubMed:10648783, ECO:0000269|PubMed:17105772, ECO:0000269|PubMed:18499658, ECO:0000269|PubMed:20124417, ECO:0000269|PubMed:21854770, ECO:0000269|PubMed:22102414, ECO:0000269|PubMed:23116066, ECO:0000269|PubMed:23797032, ECO:0000269|PubMed:26089203, ECO:0000269|PubMed:26503245, ECO:0000269|PubMed:27477908}.; FUNCTION: (Microbial infection) Required for bovine papillomavirus type 1 regulatory protein E2 loading onto mitotic chromosomes during DNA replication for the viral genome to be maintained and segregated. {ECO:0000269|PubMed:17189189}.
uniprot
proteins
mass_dalton
108313
uniprot
proteins
mutagenesis
MUTAGEN 50; /note="K->R: Loss of both DNA-dependent ATPase and ATP-dependent helicase activities, still binds ATP."; /evidence="ECO:0000269|PubMed:10648783, ECO:0000269|PubMed:18499658, ECO:0000269|PubMed:22102414"; MUTAGEN 897; /note="Missing: Loss of ATP-dependent DNA helicase and DNA-dependent ATPase activities, loss of DNA-binding, still binds ATP."; /evidence="ECO:0000269|PubMed:22102414
uniprot
proteins
protein_family
DDX11/CHL1 sub-subfamily
uniprot
proteins
protein_family
DEAD box helicase family
uniprot
proteins
protein_family
DEAH subfamily
uniprot
proteins
pubmed
10648783
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17105772
uniprot
proteins
pubmed
17189189
uniprot
proteins
pubmed
18499658
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20124417
uniprot
proteins
pubmed
20137776
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21854770
uniprot
proteins
pubmed
22102414
uniprot
proteins
pubmed
23033317
uniprot
proteins
pubmed
23116066
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23797032
uniprot
proteins
pubmed
26089203
uniprot
proteins
pubmed
26503245
uniprot
proteins
pubmed
27477908
uniprot
proteins
pubmed
32705708
uniprot
proteins
pubmed
8798685
uniprot
proteins
pubmed
9013641
uniprot
proteins
sequence_length
970
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17105772}. Nucleus, nucleolus {ECO:0000269|PubMed:17105772, ECO:0000269|PubMed:26089203, ECO:0000269|PubMed:9013641}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:17105772}. Midbody {ECO:0000269|PubMed:17105772}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17105772}. 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) (PubMed:17105772). In interphase, colocalizes with nucleolin in the nucleolus (PubMed:26089203). {ECO:0000269|PubMed:17105772, ECO:0000269|PubMed:26089203}.; SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:17189189}. Note=(Microbial infection) Colocalizes with bovine papillomavirus type 1 regulatory protein E2 on mitotic chromosomes at early stages of mitosis. {ECO:0000269|PubMed:17189189}.
uniprot
proteins