RECQ1_HUMAN
ID RECQ1_HUMAN Reviewed; 649 AA.
AC P46063; A8K6G2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 3.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=ATP-dependent DNA helicase Q1 {ECO:0000305|PubMed:7527136, ECO:0000305|PubMed:8056767};
DE EC=3.6.4.12 {ECO:0000269|PubMed:7527136, ECO:0000269|PubMed:8056767};
DE AltName: Full=DNA helicase, RecQ-like type 1;
DE Short=RecQ1;
DE AltName: Full=DNA-dependent ATPase Q1;
DE AltName: Full=RecQ protein-like 1;
GN Name=RECQL; Synonyms=RECQ1, RECQL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-38; 186-193; 293-304;
RP 396-404; 431-439 AND 594-599, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND VARIANT THR-487.
RC TISSUE=Cervix carcinoma;
RX PubMed=7961977; DOI=10.1016/s0021-9258(18)43957-9;
RA Puranam K.L., Blackshear P.J.;
RT "Cloning and characterization of RECQL, a potential human homologue of the
RT Escherichia coli DNA helicase RecQ.";
RL J. Biol. Chem. 269:29838-29845(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=7527136; DOI=10.1093/nar/22.22.4566;
RA Seki M., Miyazawa H., Tada S., Yanagisawa J., Yamaoka T., Hoshino S.,
RA Ozawa K., Eki T., Nogami M., Okumura K., Taguchi H., Hanaoka F.,
RA Enomoto T.;
RT "Molecular cloning of cDNA encoding human DNA helicase Q1 which has
RT homology to Escherichia coli Rec Q helicase and localization of the gene at
RT chromosome 12p12.";
RL Nucleic Acids Res. 22:4566-4573(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=8056767; DOI=10.1093/oxfordjournals.jbchem.a124369;
RA Seki M., Yanagisawa J., Kohda T., Sonoyama T., Ui M., Enomoto T.;
RT "Purification of two DNA-dependent adenosinetriphosphatases having DNA
RT helicase activity from HeLa cells and comparison of the properties of the
RT two enzymes.";
RL J. Biochem. 115:523-531(1994).
RN [9]
RP FUNCTION, INTERACTION WITH EXO1 AND MLH1, AND MUTAGENESIS OF LYS-119.
RX PubMed=15886194; DOI=10.1074/jbc.m500265200;
RA Doherty K.M., Sharma S., Uzdilla L.A., Wilson T.M., Cui S., Vindigni A.,
RA Brosh R.M. Jr.;
RT "RECQ1 helicase interacts with human mismatch repair factors that regulate
RT genetic recombination.";
RL J. Biol. Chem. 280:28085-28094(2005).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-514 AND LYS-522, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(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., Buerckstuemmer T.,
RA 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, AND IDENTIFICATION BY
RP 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: DNA helicase that may play a role in the repair of DNA that
CC is damaged by ultraviolet light or other mutagens. Exhibits a
CC magnesium-dependent ATP-dependent DNA-helicase activity that unwinds
CC single- and double-stranded DNA in a 3'-5' direction.
CC {ECO:0000269|PubMed:15886194, ECO:0000269|PubMed:7527136,
CC ECO:0000269|PubMed:7961977, ECO:0000269|PubMed:8056767}.
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:0000269|PubMed:7527136, ECO:0000269|PubMed:8056767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000305|PubMed:8056767};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dATP + H2O = dADP + H(+) + phosphate; Xref=Rhea:RHEA:51908,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57667, ChEBI:CHEBI:61404;
CC Evidence={ECO:0000269|PubMed:7527136, ECO:0000269|PubMed:8056767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51909;
CC Evidence={ECO:0000305|PubMed:8056767};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8056767};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:8056767};
CC -!- SUBUNIT: Interacts with EXO1 (PubMed:15886194). Interacts with MLH1.
CC {ECO:0000269|PubMed:15886194}.
CC -!- INTERACTION:
CC P46063; P52292: KPNA2; NbExp=2; IntAct=EBI-2823728, EBI-349938;
CC P46063; O00629: KPNA4; NbExp=2; IntAct=EBI-2823728, EBI-396343;
CC P46063; P09874: PARP1; NbExp=8; IntAct=EBI-2823728, EBI-355676;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7961977}.
CC -!- TISSUE SPECIFICITY: High expression in heart, lung, skeletal muscle and
CC kidney, low expression in brain. {ECO:0000269|PubMed:7961977}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60261.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RECQLID283.html";
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DR EMBL; L36140; AAA60261.1; ALT_FRAME; mRNA.
DR EMBL; D37984; BAA07200.1; -; mRNA.
DR EMBL; BT007119; AAP35783.1; -; mRNA.
DR EMBL; AK291627; BAF84316.1; -; mRNA.
DR EMBL; AC006559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96434.1; -; Genomic_DNA.
DR EMBL; BC001052; AAH01052.1; -; mRNA.
DR CCDS; CCDS31756.1; -.
DR PIR; A58836; A55311.
DR RefSeq; NP_002898.2; NM_002907.3.
DR RefSeq; NP_116559.1; NM_032941.2.
DR RefSeq; XP_005253518.1; XM_005253461.3.
DR RefSeq; XP_005253519.1; XM_005253462.4.
DR RefSeq; XP_005253520.1; XM_005253463.3.
DR RefSeq; XP_005253521.1; XM_005253464.3.
DR PDB; 2V1X; X-ray; 2.00 A; A/B=49-616.
DR PDB; 2WWY; X-ray; 2.90 A; A/B=49-616.
DR PDB; 4U7D; X-ray; 3.40 A; A/B/C/D=49-616.
DR PDB; 6JTZ; X-ray; 2.80 A; A/B=282-616.
DR PDBsum; 2V1X; -.
DR PDBsum; 2WWY; -.
DR PDBsum; 4U7D; -.
DR PDBsum; 6JTZ; -.
DR AlphaFoldDB; P46063; -.
DR SMR; P46063; -.
DR BioGRID; 111897; 86.
DR DIP; DIP-29216N; -.
DR IntAct; P46063; 43.
DR MINT; P46063; -.
DR STRING; 9606.ENSP00000416739; -.
DR BindingDB; P46063; -.
DR ChEMBL; CHEMBL1293236; -.
DR GlyGen; P46063; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P46063; -.
DR MetOSite; P46063; -.
DR PhosphoSitePlus; P46063; -.
DR SwissPalm; P46063; -.
DR BioMuta; RECQL; -.
DR DMDM; 218512113; -.
DR EPD; P46063; -.
DR jPOST; P46063; -.
DR MassIVE; P46063; -.
DR MaxQB; P46063; -.
DR PaxDb; P46063; -.
DR PeptideAtlas; P46063; -.
DR PRIDE; P46063; -.
DR ProteomicsDB; 55713; -.
DR TopDownProteomics; P46063; -.
DR Antibodypedia; 4055; 96 antibodies from 21 providers.
DR CPTC; P46063; 1 antibody.
DR DNASU; 5965; -.
DR Ensembl; ENST00000421138.6; ENSP00000395449.2; ENSG00000004700.16.
DR Ensembl; ENST00000444129.7; ENSP00000416739.2; ENSG00000004700.16.
DR GeneID; 5965; -.
DR KEGG; hsa:5965; -.
DR MANE-Select; ENST00000444129.7; ENSP00000416739.2; NM_002907.4; NP_002898.2.
DR UCSC; uc001rex.4; human.
DR CTD; 5965; -.
DR DisGeNET; 5965; -.
DR GeneCards; RECQL; -.
DR HGNC; HGNC:9948; RECQL.
DR HPA; ENSG00000004700; Low tissue specificity.
DR MalaCards; RECQL; -.
DR MIM; 600537; gene.
DR neXtProt; NX_P46063; -.
DR OpenTargets; ENSG00000004700; -.
DR PharmGKB; PA34315; -.
DR VEuPathDB; HostDB:ENSG00000004700; -.
DR eggNOG; KOG0353; Eukaryota.
DR GeneTree; ENSGT00940000157013; -.
DR HOGENOM; CLU_001103_12_5_1; -.
DR InParanoid; P46063; -.
DR OMA; FKLSTMV; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; P46063; -.
DR TreeFam; TF323555; -.
DR BRENDA; 3.6.4.12; 2681.
DR PathwayCommons; P46063; -.
DR SignaLink; P46063; -.
DR BioGRID-ORCS; 5965; 5 hits in 1075 CRISPR screens.
DR ChiTaRS; RECQL; human.
DR EvolutionaryTrace; P46063; -.
DR GeneWiki; RECQL; -.
DR GenomeRNAi; 5965; -.
DR Pharos; P46063; Tbio.
DR PRO; PR:P46063; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P46063; protein.
DR Bgee; ENSG00000004700; Expressed in buccal mucosa cell and 207 other tissues.
DR ExpressionAtlas; P46063; baseline and differential.
DR Genevisible; P46063; HS.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR GO; GO:1990814; F:DNA/DNA annealing activity; IDA:GO_Central.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Direct protein sequencing;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..649
FT /note="ATP-dependent DNA helicase Q1"
FT /id="PRO_0000205049"
FT DOMAIN 100..275
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 300..451
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 595..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 219..222
FT /note="DEVH box"
FT COMPBIAS 606..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 514
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 522
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYJ1"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VARIANT 102
FT /note="V -> I (in dbSNP:rs1065751)"
FT /id="VAR_034679"
FT VARIANT 372
FT /note="V -> I (in dbSNP:rs2230003)"
FT /id="VAR_051732"
FT VARIANT 487
FT /note="K -> T (in dbSNP:rs6501)"
FT /evidence="ECO:0000269|PubMed:7961977"
FT /id="VAR_016140"
FT VARIANT 495
FT /note="D -> H (in dbSNP:rs6499)"
FT /id="VAR_016141"
FT MUTAGEN 119
FT /note="K->A: Abrogates helicase activity."
FT /evidence="ECO:0000269|PubMed:15886194"
FT CONFLICT 1
FT /note="M -> S (in Ref. 2; BAA07200)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="A -> D (in Ref. 1; AAA60261)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="C -> S (in Ref. 1; AAA60261)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="T -> A (in Ref. 1; AAA60261)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="E -> K (in Ref. 3; AAP35783 and 7; AAH01052)"
FT /evidence="ECO:0000305"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2WWY"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 248..256
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:2V1X"
FT TURN 309..314
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 395..402
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 412..418
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 420..429
FT /evidence="ECO:0007829|PDB:2V1X"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:6JTZ"
FT HELIX 436..447
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 454..462
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 484..488
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 490..505
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 512..519
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 539..551
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 554..561
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 566..572
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 574..580
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:2V1X"
SQ SEQUENCE 649 AA; 73457 MW; F616DC3191F79391 CRC64;
MASVSALTEE LDSITSELHA VEIQIQELTE RQQELIQKKK VLTKKIKQCL EDSDAGASNE
YDSSPAAWNK EDFPWSGKVK DILQNVFKLE KFRPLQLETI NVTMAGKEVF LVMPTGGGKS
LCYQLPALCS DGFTLVICPL ISLMEDQLMV LKQLGISATM LNASSSKEHV KWVHAEMVNK
NSELKLIYVT PEKIAKSKMF MSRLEKAYEA RRFTRIAVDE VHCCSQWGHD FRPDYKALGI
LKRQFPNASL IGLTATATNH VLTDAQKILC IEKCFTFTAS FNRPNLYYEV RQKPSNTEDF
IEDIVKLING RYKGQSGIIY CFSQKDSEQV TVSLQNLGIH AGAYHANLEP EDKTTVHRKW
SANEIQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ ESGRAGRDDM KADCILYYGF
GDIFRISSMV VMENVGQQKL YEMVSYCQNI SKCRRVLMAQ HFDEVWNSEA CNKMCDNCCK
DSAFERKNIT EYCRDLIKIL KQAEELNEKL TPLKLIDSWM GKGAAKLRVA GVVAPTLPRE
DLEKIIAHFL IQQYLKEDYS FTAYATISYL KIGPKANLLN NEAHAITMQV TKSTQNSFRA
ESSQTCHSEQ GDKKMEEKNS GNFQKKAANM LQQSGSKNTG AKKRKIDDA
